Diversity of COP9 signalosome structures and functional consequences
The COP9 signalosome (CSN) is a regulator of the ubiquitin (Ub) proteasome system (UPS). It interacts with hundreds of cullin‐RING ubiquitin E3 ligases (CRLs) and regulates their activity by removing the Ub‐like protein Nedd8 from cullins. In mammalian cells 7 different cullins exist which form CRLs...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Dubiel, Dawadschargal [verfasserIn] |
|---|
| Format: |
Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2015 |
|---|
| Rechteinformationen: |
Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
|---|
| Schlagwörter: |
|---|
| Übergeordnetes Werk: |
Enthalten in: FEBS letters - Amsterdam [u.a.] : Elsevier, 1968, 589(2015), 19PartA, Seite 2507-2513 |
|---|---|
| Übergeordnetes Werk: |
volume:589 ; year:2015 ; number:19PartA ; pages:2507-2513 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.febslet.2015.06.007 |
|---|
| Katalog-ID: |
OLC1965546803 |
|---|
| LEADER | 01000caa a2200265 4500 | ||
|---|---|---|---|
| 001 | OLC1965546803 | ||
| 003 | DE-627 | ||
| 005 | 20230714164028.0 | ||
| 007 | tu | ||
| 008 | 160206s2015 xx ||||| 00| ||eng c | ||
| 024 | 7 | |a 10.1016/j.febslet.2015.06.007 |2 doi | |
| 028 | 5 | 2 | |a PQ20160617 |
| 035 | |a (DE-627)OLC1965546803 | ||
| 035 | |a (DE-599)GBVOLC1965546803 | ||
| 035 | |a (PRQ)c1940-7f64879d6d18fc9ff617f24b37eee2d0406f19b743730467040cc6b1d145f6590 | ||
| 035 | |a (KEY)0045922420150000589001902507diversityofcop9signalosomestructuresandfunctionalc | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 082 | 0 | 4 | |a 570 |a 530 |a 610 |q DNB |
| 100 | 1 | |a Dubiel, Dawadschargal |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Diversity of COP9 signalosome structures and functional consequences |
| 264 | 1 | |c 2015 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
| 338 | |a Band |b nc |2 rdacarrier | ||
| 520 | |a The COP9 signalosome (CSN) is a regulator of the ubiquitin (Ub) proteasome system (UPS). It interacts with hundreds of cullin‐RING ubiquitin E3 ligases (CRLs) and regulates their activity by removing the Ub‐like protein Nedd8 from cullins. In mammalian cells 7 different cullins exist which form CRLs with adaptor proteins and with a large number of substrate recognition subunits such as F‐box and BTB proteins. This large variety of CRL‐complexes is deneddylated by the CSN. The capacity of the CSN to interact with numerous types of CRL complexes can be explained by its structural diversity, which allows different CSN variants to interact with different binding partners and substrates and enables different subunit expression profiles. Diversity of CSN complexes presumably occurs by: (1) flexibility of CSN holo complex structure; (2) formation of CSN mini complexes and free CSN subunits and (3) generation of CSN variants via integration of CSN subunit isoforms. In this review we will discuss the structural diversity of the CSN complex and possible functional consequences. | ||
| 540 | |a Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies | ||
| 540 | |a Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | ||
| 650 | 4 | |a Deneddylation | |
| 650 | 4 | |a CSN subunit isoform | |
| 650 | 4 | |a COP9 signalosome | |
| 650 | 4 | |a CSN5 | |
| 650 | 4 | |a 3D structure | |
| 650 | 4 | |a Protein Subunits - chemistry | |
| 650 | 4 | |a Multiprotein Complexes - chemistry | |
| 650 | 4 | |a Protein Isoforms - chemistry | |
| 650 | 4 | |a Peptide Hydrolases - chemistry | |
| 700 | 1 | |a Rockel, Beate |4 oth | |
| 700 | 1 | |a Naumann, Michael |4 oth | |
| 700 | 1 | |a Dubiel, Wolfgang |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |t FEBS letters |d Amsterdam [u.a.] : Elsevier, 1968 |g 589(2015), 19PartA, Seite 2507-2513 |w (DE-627)129522023 |w (DE-600)212746-5 |w (DE-576)014938014 |x 0014-5793 |7 nnns |
| 773 | 1 | 8 | |g volume:589 |g year:2015 |g number:19PartA |g pages:2507-2513 |
| 856 | 4 | 1 | |u http://dx.doi.org/10.1016/j.febslet.2015.06.007 |3 Volltext |
| 856 | 4 | 2 | |u http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.06.007/abstract |
| 856 | 4 | 2 | |u http://www.ncbi.nlm.nih.gov/pubmed/26096786 |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a SYSFLAG_A | ||
| 912 | |a GBV_OLC | ||
| 912 | |a SSG-OLC-PHY | ||
| 912 | |a SSG-OLC-CHE | ||
| 912 | |a SSG-OLC-PHA | ||
| 912 | |a SSG-OLC-DE-84 | ||
| 912 | |a GBV_ILN_21 | ||
| 912 | |a GBV_ILN_70 | ||
| 912 | |a GBV_ILN_211 | ||
| 912 | |a GBV_ILN_2219 | ||
| 912 | |a GBV_ILN_4012 | ||
| 912 | |a GBV_ILN_4125 | ||
| 912 | |a GBV_ILN_4219 | ||
| 912 | |a GBV_ILN_4305 | ||
| 951 | |a AR | ||
| 952 | |d 589 |j 2015 |e 19PartA |h 2507-2513 | ||
| author_variant |
d d dd |
|---|---|
| matchkey_str |
article:00145793:2015----::iestocpsgaooetutrsnfnt |
| hierarchy_sort_str |
2015 |
| publishDate |
2015 |
| allfields |
10.1016/j.febslet.2015.06.007 doi PQ20160617 (DE-627)OLC1965546803 (DE-599)GBVOLC1965546803 (PRQ)c1940-7f64879d6d18fc9ff617f24b37eee2d0406f19b743730467040cc6b1d145f6590 (KEY)0045922420150000589001902507diversityofcop9signalosomestructuresandfunctionalc DE-627 ger DE-627 rakwb eng 570 530 610 DNB Dubiel, Dawadschargal verfasserin aut Diversity of COP9 signalosome structures and functional consequences 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The COP9 signalosome (CSN) is a regulator of the ubiquitin (Ub) proteasome system (UPS). It interacts with hundreds of cullin‐RING ubiquitin E3 ligases (CRLs) and regulates their activity by removing the Ub‐like protein Nedd8 from cullins. In mammalian cells 7 different cullins exist which form CRLs with adaptor proteins and with a large number of substrate recognition subunits such as F‐box and BTB proteins. This large variety of CRL‐complexes is deneddylated by the CSN. The capacity of the CSN to interact with numerous types of CRL complexes can be explained by its structural diversity, which allows different CSN variants to interact with different binding partners and substrates and enables different subunit expression profiles. Diversity of CSN complexes presumably occurs by: (1) flexibility of CSN holo complex structure; (2) formation of CSN mini complexes and free CSN subunits and (3) generation of CSN variants via integration of CSN subunit isoforms. In this review we will discuss the structural diversity of the CSN complex and possible functional consequences. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Deneddylation CSN subunit isoform COP9 signalosome CSN5 3D structure Protein Subunits - chemistry Multiprotein Complexes - chemistry Protein Isoforms - chemistry Peptide Hydrolases - chemistry Rockel, Beate oth Naumann, Michael oth Dubiel, Wolfgang oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 19PartA, Seite 2507-2513 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:19PartA pages:2507-2513 http://dx.doi.org/10.1016/j.febslet.2015.06.007 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.06.007/abstract http://www.ncbi.nlm.nih.gov/pubmed/26096786 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 19PartA 2507-2513 |
| spelling |
10.1016/j.febslet.2015.06.007 doi PQ20160617 (DE-627)OLC1965546803 (DE-599)GBVOLC1965546803 (PRQ)c1940-7f64879d6d18fc9ff617f24b37eee2d0406f19b743730467040cc6b1d145f6590 (KEY)0045922420150000589001902507diversityofcop9signalosomestructuresandfunctionalc DE-627 ger DE-627 rakwb eng 570 530 610 DNB Dubiel, Dawadschargal verfasserin aut Diversity of COP9 signalosome structures and functional consequences 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The COP9 signalosome (CSN) is a regulator of the ubiquitin (Ub) proteasome system (UPS). It interacts with hundreds of cullin‐RING ubiquitin E3 ligases (CRLs) and regulates their activity by removing the Ub‐like protein Nedd8 from cullins. In mammalian cells 7 different cullins exist which form CRLs with adaptor proteins and with a large number of substrate recognition subunits such as F‐box and BTB proteins. This large variety of CRL‐complexes is deneddylated by the CSN. The capacity of the CSN to interact with numerous types of CRL complexes can be explained by its structural diversity, which allows different CSN variants to interact with different binding partners and substrates and enables different subunit expression profiles. Diversity of CSN complexes presumably occurs by: (1) flexibility of CSN holo complex structure; (2) formation of CSN mini complexes and free CSN subunits and (3) generation of CSN variants via integration of CSN subunit isoforms. In this review we will discuss the structural diversity of the CSN complex and possible functional consequences. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Deneddylation CSN subunit isoform COP9 signalosome CSN5 3D structure Protein Subunits - chemistry Multiprotein Complexes - chemistry Protein Isoforms - chemistry Peptide Hydrolases - chemistry Rockel, Beate oth Naumann, Michael oth Dubiel, Wolfgang oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 19PartA, Seite 2507-2513 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:19PartA pages:2507-2513 http://dx.doi.org/10.1016/j.febslet.2015.06.007 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.06.007/abstract http://www.ncbi.nlm.nih.gov/pubmed/26096786 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 19PartA 2507-2513 |
| allfields_unstemmed |
10.1016/j.febslet.2015.06.007 doi PQ20160617 (DE-627)OLC1965546803 (DE-599)GBVOLC1965546803 (PRQ)c1940-7f64879d6d18fc9ff617f24b37eee2d0406f19b743730467040cc6b1d145f6590 (KEY)0045922420150000589001902507diversityofcop9signalosomestructuresandfunctionalc DE-627 ger DE-627 rakwb eng 570 530 610 DNB Dubiel, Dawadschargal verfasserin aut Diversity of COP9 signalosome structures and functional consequences 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The COP9 signalosome (CSN) is a regulator of the ubiquitin (Ub) proteasome system (UPS). It interacts with hundreds of cullin‐RING ubiquitin E3 ligases (CRLs) and regulates their activity by removing the Ub‐like protein Nedd8 from cullins. In mammalian cells 7 different cullins exist which form CRLs with adaptor proteins and with a large number of substrate recognition subunits such as F‐box and BTB proteins. This large variety of CRL‐complexes is deneddylated by the CSN. The capacity of the CSN to interact with numerous types of CRL complexes can be explained by its structural diversity, which allows different CSN variants to interact with different binding partners and substrates and enables different subunit expression profiles. Diversity of CSN complexes presumably occurs by: (1) flexibility of CSN holo complex structure; (2) formation of CSN mini complexes and free CSN subunits and (3) generation of CSN variants via integration of CSN subunit isoforms. In this review we will discuss the structural diversity of the CSN complex and possible functional consequences. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Deneddylation CSN subunit isoform COP9 signalosome CSN5 3D structure Protein Subunits - chemistry Multiprotein Complexes - chemistry Protein Isoforms - chemistry Peptide Hydrolases - chemistry Rockel, Beate oth Naumann, Michael oth Dubiel, Wolfgang oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 19PartA, Seite 2507-2513 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:19PartA pages:2507-2513 http://dx.doi.org/10.1016/j.febslet.2015.06.007 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.06.007/abstract http://www.ncbi.nlm.nih.gov/pubmed/26096786 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 19PartA 2507-2513 |
| allfieldsGer |
10.1016/j.febslet.2015.06.007 doi PQ20160617 (DE-627)OLC1965546803 (DE-599)GBVOLC1965546803 (PRQ)c1940-7f64879d6d18fc9ff617f24b37eee2d0406f19b743730467040cc6b1d145f6590 (KEY)0045922420150000589001902507diversityofcop9signalosomestructuresandfunctionalc DE-627 ger DE-627 rakwb eng 570 530 610 DNB Dubiel, Dawadschargal verfasserin aut Diversity of COP9 signalosome structures and functional consequences 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The COP9 signalosome (CSN) is a regulator of the ubiquitin (Ub) proteasome system (UPS). It interacts with hundreds of cullin‐RING ubiquitin E3 ligases (CRLs) and regulates their activity by removing the Ub‐like protein Nedd8 from cullins. In mammalian cells 7 different cullins exist which form CRLs with adaptor proteins and with a large number of substrate recognition subunits such as F‐box and BTB proteins. This large variety of CRL‐complexes is deneddylated by the CSN. The capacity of the CSN to interact with numerous types of CRL complexes can be explained by its structural diversity, which allows different CSN variants to interact with different binding partners and substrates and enables different subunit expression profiles. Diversity of CSN complexes presumably occurs by: (1) flexibility of CSN holo complex structure; (2) formation of CSN mini complexes and free CSN subunits and (3) generation of CSN variants via integration of CSN subunit isoforms. In this review we will discuss the structural diversity of the CSN complex and possible functional consequences. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Deneddylation CSN subunit isoform COP9 signalosome CSN5 3D structure Protein Subunits - chemistry Multiprotein Complexes - chemistry Protein Isoforms - chemistry Peptide Hydrolases - chemistry Rockel, Beate oth Naumann, Michael oth Dubiel, Wolfgang oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 19PartA, Seite 2507-2513 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:19PartA pages:2507-2513 http://dx.doi.org/10.1016/j.febslet.2015.06.007 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.06.007/abstract http://www.ncbi.nlm.nih.gov/pubmed/26096786 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 19PartA 2507-2513 |
| allfieldsSound |
10.1016/j.febslet.2015.06.007 doi PQ20160617 (DE-627)OLC1965546803 (DE-599)GBVOLC1965546803 (PRQ)c1940-7f64879d6d18fc9ff617f24b37eee2d0406f19b743730467040cc6b1d145f6590 (KEY)0045922420150000589001902507diversityofcop9signalosomestructuresandfunctionalc DE-627 ger DE-627 rakwb eng 570 530 610 DNB Dubiel, Dawadschargal verfasserin aut Diversity of COP9 signalosome structures and functional consequences 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The COP9 signalosome (CSN) is a regulator of the ubiquitin (Ub) proteasome system (UPS). It interacts with hundreds of cullin‐RING ubiquitin E3 ligases (CRLs) and regulates their activity by removing the Ub‐like protein Nedd8 from cullins. In mammalian cells 7 different cullins exist which form CRLs with adaptor proteins and with a large number of substrate recognition subunits such as F‐box and BTB proteins. This large variety of CRL‐complexes is deneddylated by the CSN. The capacity of the CSN to interact with numerous types of CRL complexes can be explained by its structural diversity, which allows different CSN variants to interact with different binding partners and substrates and enables different subunit expression profiles. Diversity of CSN complexes presumably occurs by: (1) flexibility of CSN holo complex structure; (2) formation of CSN mini complexes and free CSN subunits and (3) generation of CSN variants via integration of CSN subunit isoforms. In this review we will discuss the structural diversity of the CSN complex and possible functional consequences. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Deneddylation CSN subunit isoform COP9 signalosome CSN5 3D structure Protein Subunits - chemistry Multiprotein Complexes - chemistry Protein Isoforms - chemistry Peptide Hydrolases - chemistry Rockel, Beate oth Naumann, Michael oth Dubiel, Wolfgang oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 19PartA, Seite 2507-2513 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:19PartA pages:2507-2513 http://dx.doi.org/10.1016/j.febslet.2015.06.007 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.06.007/abstract http://www.ncbi.nlm.nih.gov/pubmed/26096786 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 19PartA 2507-2513 |
| language |
English |
| source |
Enthalten in FEBS letters 589(2015), 19PartA, Seite 2507-2513 volume:589 year:2015 number:19PartA pages:2507-2513 |
| sourceStr |
Enthalten in FEBS letters 589(2015), 19PartA, Seite 2507-2513 volume:589 year:2015 number:19PartA pages:2507-2513 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| topic_facet |
Deneddylation CSN subunit isoform COP9 signalosome CSN5 3D structure Protein Subunits - chemistry Multiprotein Complexes - chemistry Protein Isoforms - chemistry Peptide Hydrolases - chemistry |
| dewey-raw |
570 |
| isfreeaccess_bool |
false |
| container_title |
FEBS letters |
| authorswithroles_txt_mv |
Dubiel, Dawadschargal @@aut@@ Rockel, Beate @@oth@@ Naumann, Michael @@oth@@ Dubiel, Wolfgang @@oth@@ |
| publishDateDaySort_date |
2015-01-01T00:00:00Z |
| hierarchy_top_id |
129522023 |
| dewey-sort |
3570 |
| id |
OLC1965546803 |
| language_de |
englisch |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a2200265 4500</leader><controlfield tag="001">OLC1965546803</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230714164028.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">160206s2015 xx ||||| 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.febslet.2015.06.007</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">PQ20160617</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC1965546803</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVOLC1965546803</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(PRQ)c1940-7f64879d6d18fc9ff617f24b37eee2d0406f19b743730467040cc6b1d145f6590</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(KEY)0045922420150000589001902507diversityofcop9signalosomestructuresandfunctionalc</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="a">530</subfield><subfield code="a">610</subfield><subfield code="q">DNB</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Dubiel, Dawadschargal</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Diversity of COP9 signalosome structures and functional consequences</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2015</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The COP9 signalosome (CSN) is a regulator of the ubiquitin (Ub) proteasome system (UPS). It interacts with hundreds of cullin‐RING ubiquitin E3 ligases (CRLs) and regulates their activity by removing the Ub‐like protein Nedd8 from cullins. In mammalian cells 7 different cullins exist which form CRLs with adaptor proteins and with a large number of substrate recognition subunits such as F‐box and BTB proteins. This large variety of CRL‐complexes is deneddylated by the CSN. The capacity of the CSN to interact with numerous types of CRL complexes can be explained by its structural diversity, which allows different CSN variants to interact with different binding partners and substrates and enables different subunit expression profiles. Diversity of CSN complexes presumably occurs by: (1) flexibility of CSN holo complex structure; (2) formation of CSN mini complexes and free CSN subunits and (3) generation of CSN variants via integration of CSN subunit isoforms. In this review we will discuss the structural diversity of the CSN complex and possible functional consequences.</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Deneddylation</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">CSN subunit isoform</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">COP9 signalosome</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">CSN5</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">3D structure</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protein Subunits - chemistry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Multiprotein Complexes - chemistry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protein Isoforms - chemistry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Peptide Hydrolases - chemistry</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Rockel, Beate</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Naumann, Michael</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Dubiel, Wolfgang</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">FEBS letters</subfield><subfield code="d">Amsterdam [u.a.] : Elsevier, 1968</subfield><subfield code="g">589(2015), 19PartA, Seite 2507-2513</subfield><subfield code="w">(DE-627)129522023</subfield><subfield code="w">(DE-600)212746-5</subfield><subfield code="w">(DE-576)014938014</subfield><subfield code="x">0014-5793</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:589</subfield><subfield code="g">year:2015</subfield><subfield code="g">number:19PartA</subfield><subfield code="g">pages:2507-2513</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">http://dx.doi.org/10.1016/j.febslet.2015.06.007</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.06.007/abstract</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.ncbi.nlm.nih.gov/pubmed/26096786</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHY</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-DE-84</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_21</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_211</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2219</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4125</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4219</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4305</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">589</subfield><subfield code="j">2015</subfield><subfield code="e">19PartA</subfield><subfield code="h">2507-2513</subfield></datafield></record></collection>
|
| author |
Dubiel, Dawadschargal |
| spellingShingle |
Dubiel, Dawadschargal ddc 570 misc Deneddylation misc CSN subunit isoform misc COP9 signalosome misc CSN5 misc 3D structure misc Protein Subunits - chemistry misc Multiprotein Complexes - chemistry misc Protein Isoforms - chemistry misc Peptide Hydrolases - chemistry Diversity of COP9 signalosome structures and functional consequences |
| authorStr |
Dubiel, Dawadschargal |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)129522023 |
| format |
Article |
| dewey-ones |
570 - Life sciences; biology 530 - Physics 610 - Medicine & health |
| delete_txt_mv |
keep |
| author_role |
aut |
| collection |
OLC |
| remote_str |
false |
| illustrated |
Not Illustrated |
| issn |
0014-5793 |
| topic_title |
570 530 610 DNB Diversity of COP9 signalosome structures and functional consequences Deneddylation CSN subunit isoform COP9 signalosome CSN5 3D structure Protein Subunits - chemistry Multiprotein Complexes - chemistry Protein Isoforms - chemistry Peptide Hydrolases - chemistry |
| topic |
ddc 570 misc Deneddylation misc CSN subunit isoform misc COP9 signalosome misc CSN5 misc 3D structure misc Protein Subunits - chemistry misc Multiprotein Complexes - chemistry misc Protein Isoforms - chemistry misc Peptide Hydrolases - chemistry |
| topic_unstemmed |
ddc 570 misc Deneddylation misc CSN subunit isoform misc COP9 signalosome misc CSN5 misc 3D structure misc Protein Subunits - chemistry misc Multiprotein Complexes - chemistry misc Protein Isoforms - chemistry misc Peptide Hydrolases - chemistry |
| topic_browse |
ddc 570 misc Deneddylation misc CSN subunit isoform misc COP9 signalosome misc CSN5 misc 3D structure misc Protein Subunits - chemistry misc Multiprotein Complexes - chemistry misc Protein Isoforms - chemistry misc Peptide Hydrolases - chemistry |
| format_facet |
Aufsätze Gedruckte Aufsätze |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
nc |
| author2_variant |
b r br m n mn w d wd |
| hierarchy_parent_title |
FEBS letters |
| hierarchy_parent_id |
129522023 |
| dewey-tens |
570 - Life sciences; biology 530 - Physics 610 - Medicine & health |
| hierarchy_top_title |
FEBS letters |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 |
| title |
Diversity of COP9 signalosome structures and functional consequences |
| ctrlnum |
(DE-627)OLC1965546803 (DE-599)GBVOLC1965546803 (PRQ)c1940-7f64879d6d18fc9ff617f24b37eee2d0406f19b743730467040cc6b1d145f6590 (KEY)0045922420150000589001902507diversityofcop9signalosomestructuresandfunctionalc |
| title_full |
Diversity of COP9 signalosome structures and functional consequences |
| author_sort |
Dubiel, Dawadschargal |
| journal |
FEBS letters |
| journalStr |
FEBS letters |
| lang_code |
eng |
| isOA_bool |
false |
| dewey-hundreds |
500 - Science 600 - Technology |
| recordtype |
marc |
| publishDateSort |
2015 |
| contenttype_str_mv |
txt |
| container_start_page |
2507 |
| author_browse |
Dubiel, Dawadschargal |
| container_volume |
589 |
| class |
570 530 610 DNB |
| format_se |
Aufsätze |
| author-letter |
Dubiel, Dawadschargal |
| doi_str_mv |
10.1016/j.febslet.2015.06.007 |
| dewey-full |
570 530 610 |
| title_sort |
diversity of cop9 signalosome structures and functional consequences |
| title_auth |
Diversity of COP9 signalosome structures and functional consequences |
| abstract |
The COP9 signalosome (CSN) is a regulator of the ubiquitin (Ub) proteasome system (UPS). It interacts with hundreds of cullin‐RING ubiquitin E3 ligases (CRLs) and regulates their activity by removing the Ub‐like protein Nedd8 from cullins. In mammalian cells 7 different cullins exist which form CRLs with adaptor proteins and with a large number of substrate recognition subunits such as F‐box and BTB proteins. This large variety of CRL‐complexes is deneddylated by the CSN. The capacity of the CSN to interact with numerous types of CRL complexes can be explained by its structural diversity, which allows different CSN variants to interact with different binding partners and substrates and enables different subunit expression profiles. Diversity of CSN complexes presumably occurs by: (1) flexibility of CSN holo complex structure; (2) formation of CSN mini complexes and free CSN subunits and (3) generation of CSN variants via integration of CSN subunit isoforms. In this review we will discuss the structural diversity of the CSN complex and possible functional consequences. |
| abstractGer |
The COP9 signalosome (CSN) is a regulator of the ubiquitin (Ub) proteasome system (UPS). It interacts with hundreds of cullin‐RING ubiquitin E3 ligases (CRLs) and regulates their activity by removing the Ub‐like protein Nedd8 from cullins. In mammalian cells 7 different cullins exist which form CRLs with adaptor proteins and with a large number of substrate recognition subunits such as F‐box and BTB proteins. This large variety of CRL‐complexes is deneddylated by the CSN. The capacity of the CSN to interact with numerous types of CRL complexes can be explained by its structural diversity, which allows different CSN variants to interact with different binding partners and substrates and enables different subunit expression profiles. Diversity of CSN complexes presumably occurs by: (1) flexibility of CSN holo complex structure; (2) formation of CSN mini complexes and free CSN subunits and (3) generation of CSN variants via integration of CSN subunit isoforms. In this review we will discuss the structural diversity of the CSN complex and possible functional consequences. |
| abstract_unstemmed |
The COP9 signalosome (CSN) is a regulator of the ubiquitin (Ub) proteasome system (UPS). It interacts with hundreds of cullin‐RING ubiquitin E3 ligases (CRLs) and regulates their activity by removing the Ub‐like protein Nedd8 from cullins. In mammalian cells 7 different cullins exist which form CRLs with adaptor proteins and with a large number of substrate recognition subunits such as F‐box and BTB proteins. This large variety of CRL‐complexes is deneddylated by the CSN. The capacity of the CSN to interact with numerous types of CRL complexes can be explained by its structural diversity, which allows different CSN variants to interact with different binding partners and substrates and enables different subunit expression profiles. Diversity of CSN complexes presumably occurs by: (1) flexibility of CSN holo complex structure; (2) formation of CSN mini complexes and free CSN subunits and (3) generation of CSN variants via integration of CSN subunit isoforms. In this review we will discuss the structural diversity of the CSN complex and possible functional consequences. |
| collection_details |
GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 |
| container_issue |
19PartA |
| title_short |
Diversity of COP9 signalosome structures and functional consequences |
| url |
http://dx.doi.org/10.1016/j.febslet.2015.06.007 http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.06.007/abstract http://www.ncbi.nlm.nih.gov/pubmed/26096786 |
| remote_bool |
false |
| author2 |
Rockel, Beate Naumann, Michael Dubiel, Wolfgang |
| author2Str |
Rockel, Beate Naumann, Michael Dubiel, Wolfgang |
| ppnlink |
129522023 |
| mediatype_str_mv |
n |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth oth oth |
| doi_str |
10.1016/j.febslet.2015.06.007 |
| up_date |
2024-07-03T18:13:35.222Z |
| _version_ |
1803582612674969600 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a2200265 4500</leader><controlfield tag="001">OLC1965546803</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230714164028.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">160206s2015 xx ||||| 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.febslet.2015.06.007</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">PQ20160617</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC1965546803</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVOLC1965546803</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(PRQ)c1940-7f64879d6d18fc9ff617f24b37eee2d0406f19b743730467040cc6b1d145f6590</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(KEY)0045922420150000589001902507diversityofcop9signalosomestructuresandfunctionalc</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="a">530</subfield><subfield code="a">610</subfield><subfield code="q">DNB</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Dubiel, Dawadschargal</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Diversity of COP9 signalosome structures and functional consequences</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2015</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The COP9 signalosome (CSN) is a regulator of the ubiquitin (Ub) proteasome system (UPS). It interacts with hundreds of cullin‐RING ubiquitin E3 ligases (CRLs) and regulates their activity by removing the Ub‐like protein Nedd8 from cullins. In mammalian cells 7 different cullins exist which form CRLs with adaptor proteins and with a large number of substrate recognition subunits such as F‐box and BTB proteins. This large variety of CRL‐complexes is deneddylated by the CSN. The capacity of the CSN to interact with numerous types of CRL complexes can be explained by its structural diversity, which allows different CSN variants to interact with different binding partners and substrates and enables different subunit expression profiles. Diversity of CSN complexes presumably occurs by: (1) flexibility of CSN holo complex structure; (2) formation of CSN mini complexes and free CSN subunits and (3) generation of CSN variants via integration of CSN subunit isoforms. In this review we will discuss the structural diversity of the CSN complex and possible functional consequences.</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Deneddylation</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">CSN subunit isoform</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">COP9 signalosome</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">CSN5</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">3D structure</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protein Subunits - chemistry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Multiprotein Complexes - chemistry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protein Isoforms - chemistry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Peptide Hydrolases - chemistry</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Rockel, Beate</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Naumann, Michael</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Dubiel, Wolfgang</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">FEBS letters</subfield><subfield code="d">Amsterdam [u.a.] : Elsevier, 1968</subfield><subfield code="g">589(2015), 19PartA, Seite 2507-2513</subfield><subfield code="w">(DE-627)129522023</subfield><subfield code="w">(DE-600)212746-5</subfield><subfield code="w">(DE-576)014938014</subfield><subfield code="x">0014-5793</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:589</subfield><subfield code="g">year:2015</subfield><subfield code="g">number:19PartA</subfield><subfield code="g">pages:2507-2513</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">http://dx.doi.org/10.1016/j.febslet.2015.06.007</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.06.007/abstract</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.ncbi.nlm.nih.gov/pubmed/26096786</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHY</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-DE-84</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_21</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_211</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2219</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4125</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4219</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4305</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">589</subfield><subfield code="j">2015</subfield><subfield code="e">19PartA</subfield><subfield code="h">2507-2513</subfield></datafield></record></collection>
|
| score |
7.4017286 |