"Cullin 4 makes its mark on chromatin"

Abstract Cullin 4 (Cul4), a member of the evolutionally conserved cullin protein family, serves as a scaffold to assemble multisubunit ubiquitin E3 ligase complexes. Cul4 interacts with the Ring finger-containing protein ROC1 through its C-terminal cullin domain and with substrate recruiting subunit...
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Autor*in:	Dai, Qian [verfasserIn] Wang, Hengbin

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2006

Schlagwörter:	Nucleotide Excision Repair Ubiquitin Ligase Activity Nucleotide Excision Repair Pathway Damage Focus Histone Ubiquitylation

Anmerkung:	© Dai and Wang; licensee BioMed Central Ltd. 2006

Übergeordnetes Werk:	Enthalten in: Cell division - London : BioMed Central, 2006, 1(2006), 1 vom: 10. Juli
Übergeordnetes Werk:	volume:1 ; year:2006 ; number:1 ; day:10 ; month:07

Links:	Volltext

DOI / URN:	10.1186/1747-1028-1-14

Katalog-ID:	SPR029412838

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520			\|a Abstract Cullin 4 (Cul4), a member of the evolutionally conserved cullin protein family, serves as a scaffold to assemble multisubunit ubiquitin E3 ligase complexes. Cul4 interacts with the Ring finger-containing protein ROC1 through its C-terminal cullin domain and with substrate recruiting subunit(s) through its N-terminus. Previous studies have demonstrated that Cul4 E3 ligase ubiquitylates key regulators in cell cycle control and mediates their degradation through the proteasomal pathway, thus contributing to genome stability. Recent studies from several groups have revealed that Cul4 E3 ligase can target histones for ubiquitylation, and importantly, ubiquitylation of histones may facilitate the cellular response to DNA damage. Therefore, histone ubiquitylation by Cul4 E3 ligase constitutes a novel mechanism through which Cul4 regulates chromatin function and maintains genomic integrity. We outline these studies and suggest that histone ubiquitylation might play important roles in Cul4-regualted chromatin function including the cellular response to DNA damage and heterochromatin gene silencing.
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allfields	10.1186/1747-1028-1-14 doi (DE-627)SPR029412838 (SPR)1747-1028-1-14-e DE-627 ger DE-627 rakwb eng Dai, Qian verfasserin aut "Cullin 4 makes its mark on chromatin" 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Dai and Wang; licensee BioMed Central Ltd. 2006 Abstract Cullin 4 (Cul4), a member of the evolutionally conserved cullin protein family, serves as a scaffold to assemble multisubunit ubiquitin E3 ligase complexes. Cul4 interacts with the Ring finger-containing protein ROC1 through its C-terminal cullin domain and with substrate recruiting subunit(s) through its N-terminus. Previous studies have demonstrated that Cul4 E3 ligase ubiquitylates key regulators in cell cycle control and mediates their degradation through the proteasomal pathway, thus contributing to genome stability. Recent studies from several groups have revealed that Cul4 E3 ligase can target histones for ubiquitylation, and importantly, ubiquitylation of histones may facilitate the cellular response to DNA damage. Therefore, histone ubiquitylation by Cul4 E3 ligase constitutes a novel mechanism through which Cul4 regulates chromatin function and maintains genomic integrity. We outline these studies and suggest that histone ubiquitylation might play important roles in Cul4-regualted chromatin function including the cellular response to DNA damage and heterochromatin gene silencing. Nucleotide Excision Repair (dpeaa)DE-He213 Ubiquitin Ligase Activity (dpeaa)DE-He213 Nucleotide Excision Repair Pathway (dpeaa)DE-He213 Damage Focus (dpeaa)DE-He213 Histone Ubiquitylation (dpeaa)DE-He213 Wang, Hengbin aut Enthalten in Cell division London : BioMed Central, 2006 1(2006), 1 vom: 10. Juli (DE-627)512300607 (DE-600)2236097-9 1747-1028 nnns volume:1 year:2006 number:1 day:10 month:07 https://dx.doi.org/10.1186/1747-1028-1-14 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 1 2006 1 10 07
spelling	10.1186/1747-1028-1-14 doi (DE-627)SPR029412838 (SPR)1747-1028-1-14-e DE-627 ger DE-627 rakwb eng Dai, Qian verfasserin aut "Cullin 4 makes its mark on chromatin" 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Dai and Wang; licensee BioMed Central Ltd. 2006 Abstract Cullin 4 (Cul4), a member of the evolutionally conserved cullin protein family, serves as a scaffold to assemble multisubunit ubiquitin E3 ligase complexes. Cul4 interacts with the Ring finger-containing protein ROC1 through its C-terminal cullin domain and with substrate recruiting subunit(s) through its N-terminus. Previous studies have demonstrated that Cul4 E3 ligase ubiquitylates key regulators in cell cycle control and mediates their degradation through the proteasomal pathway, thus contributing to genome stability. Recent studies from several groups have revealed that Cul4 E3 ligase can target histones for ubiquitylation, and importantly, ubiquitylation of histones may facilitate the cellular response to DNA damage. Therefore, histone ubiquitylation by Cul4 E3 ligase constitutes a novel mechanism through which Cul4 regulates chromatin function and maintains genomic integrity. We outline these studies and suggest that histone ubiquitylation might play important roles in Cul4-regualted chromatin function including the cellular response to DNA damage and heterochromatin gene silencing. Nucleotide Excision Repair (dpeaa)DE-He213 Ubiquitin Ligase Activity (dpeaa)DE-He213 Nucleotide Excision Repair Pathway (dpeaa)DE-He213 Damage Focus (dpeaa)DE-He213 Histone Ubiquitylation (dpeaa)DE-He213 Wang, Hengbin aut Enthalten in Cell division London : BioMed Central, 2006 1(2006), 1 vom: 10. Juli (DE-627)512300607 (DE-600)2236097-9 1747-1028 nnns volume:1 year:2006 number:1 day:10 month:07 https://dx.doi.org/10.1186/1747-1028-1-14 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 1 2006 1 10 07
allfields_unstemmed	10.1186/1747-1028-1-14 doi (DE-627)SPR029412838 (SPR)1747-1028-1-14-e DE-627 ger DE-627 rakwb eng Dai, Qian verfasserin aut "Cullin 4 makes its mark on chromatin" 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Dai and Wang; licensee BioMed Central Ltd. 2006 Abstract Cullin 4 (Cul4), a member of the evolutionally conserved cullin protein family, serves as a scaffold to assemble multisubunit ubiquitin E3 ligase complexes. Cul4 interacts with the Ring finger-containing protein ROC1 through its C-terminal cullin domain and with substrate recruiting subunit(s) through its N-terminus. Previous studies have demonstrated that Cul4 E3 ligase ubiquitylates key regulators in cell cycle control and mediates their degradation through the proteasomal pathway, thus contributing to genome stability. Recent studies from several groups have revealed that Cul4 E3 ligase can target histones for ubiquitylation, and importantly, ubiquitylation of histones may facilitate the cellular response to DNA damage. Therefore, histone ubiquitylation by Cul4 E3 ligase constitutes a novel mechanism through which Cul4 regulates chromatin function and maintains genomic integrity. We outline these studies and suggest that histone ubiquitylation might play important roles in Cul4-regualted chromatin function including the cellular response to DNA damage and heterochromatin gene silencing. Nucleotide Excision Repair (dpeaa)DE-He213 Ubiquitin Ligase Activity (dpeaa)DE-He213 Nucleotide Excision Repair Pathway (dpeaa)DE-He213 Damage Focus (dpeaa)DE-He213 Histone Ubiquitylation (dpeaa)DE-He213 Wang, Hengbin aut Enthalten in Cell division London : BioMed Central, 2006 1(2006), 1 vom: 10. Juli (DE-627)512300607 (DE-600)2236097-9 1747-1028 nnns volume:1 year:2006 number:1 day:10 month:07 https://dx.doi.org/10.1186/1747-1028-1-14 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 1 2006 1 10 07
allfieldsGer	10.1186/1747-1028-1-14 doi (DE-627)SPR029412838 (SPR)1747-1028-1-14-e DE-627 ger DE-627 rakwb eng Dai, Qian verfasserin aut "Cullin 4 makes its mark on chromatin" 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Dai and Wang; licensee BioMed Central Ltd. 2006 Abstract Cullin 4 (Cul4), a member of the evolutionally conserved cullin protein family, serves as a scaffold to assemble multisubunit ubiquitin E3 ligase complexes. Cul4 interacts with the Ring finger-containing protein ROC1 through its C-terminal cullin domain and with substrate recruiting subunit(s) through its N-terminus. Previous studies have demonstrated that Cul4 E3 ligase ubiquitylates key regulators in cell cycle control and mediates their degradation through the proteasomal pathway, thus contributing to genome stability. Recent studies from several groups have revealed that Cul4 E3 ligase can target histones for ubiquitylation, and importantly, ubiquitylation of histones may facilitate the cellular response to DNA damage. Therefore, histone ubiquitylation by Cul4 E3 ligase constitutes a novel mechanism through which Cul4 regulates chromatin function and maintains genomic integrity. We outline these studies and suggest that histone ubiquitylation might play important roles in Cul4-regualted chromatin function including the cellular response to DNA damage and heterochromatin gene silencing. Nucleotide Excision Repair (dpeaa)DE-He213 Ubiquitin Ligase Activity (dpeaa)DE-He213 Nucleotide Excision Repair Pathway (dpeaa)DE-He213 Damage Focus (dpeaa)DE-He213 Histone Ubiquitylation (dpeaa)DE-He213 Wang, Hengbin aut Enthalten in Cell division London : BioMed Central, 2006 1(2006), 1 vom: 10. Juli (DE-627)512300607 (DE-600)2236097-9 1747-1028 nnns volume:1 year:2006 number:1 day:10 month:07 https://dx.doi.org/10.1186/1747-1028-1-14 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 1 2006 1 10 07
allfieldsSound	10.1186/1747-1028-1-14 doi (DE-627)SPR029412838 (SPR)1747-1028-1-14-e DE-627 ger DE-627 rakwb eng Dai, Qian verfasserin aut "Cullin 4 makes its mark on chromatin" 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Dai and Wang; licensee BioMed Central Ltd. 2006 Abstract Cullin 4 (Cul4), a member of the evolutionally conserved cullin protein family, serves as a scaffold to assemble multisubunit ubiquitin E3 ligase complexes. Cul4 interacts with the Ring finger-containing protein ROC1 through its C-terminal cullin domain and with substrate recruiting subunit(s) through its N-terminus. Previous studies have demonstrated that Cul4 E3 ligase ubiquitylates key regulators in cell cycle control and mediates their degradation through the proteasomal pathway, thus contributing to genome stability. Recent studies from several groups have revealed that Cul4 E3 ligase can target histones for ubiquitylation, and importantly, ubiquitylation of histones may facilitate the cellular response to DNA damage. Therefore, histone ubiquitylation by Cul4 E3 ligase constitutes a novel mechanism through which Cul4 regulates chromatin function and maintains genomic integrity. We outline these studies and suggest that histone ubiquitylation might play important roles in Cul4-regualted chromatin function including the cellular response to DNA damage and heterochromatin gene silencing. Nucleotide Excision Repair (dpeaa)DE-He213 Ubiquitin Ligase Activity (dpeaa)DE-He213 Nucleotide Excision Repair Pathway (dpeaa)DE-He213 Damage Focus (dpeaa)DE-He213 Histone Ubiquitylation (dpeaa)DE-He213 Wang, Hengbin aut Enthalten in Cell division London : BioMed Central, 2006 1(2006), 1 vom: 10. Juli (DE-627)512300607 (DE-600)2236097-9 1747-1028 nnns volume:1 year:2006 number:1 day:10 month:07 https://dx.doi.org/10.1186/1747-1028-1-14 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 1 2006 1 10 07
language	English
source	Enthalten in Cell division 1(2006), 1 vom: 10. Juli volume:1 year:2006 number:1 day:10 month:07
sourceStr	Enthalten in Cell division 1(2006), 1 vom: 10. Juli volume:1 year:2006 number:1 day:10 month:07
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Nucleotide Excision Repair Ubiquitin Ligase Activity Nucleotide Excision Repair Pathway Damage Focus Histone Ubiquitylation
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container_title	Cell division
authorswithroles_txt_mv	Dai, Qian @@aut@@ Wang, Hengbin @@aut@@
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author	Dai, Qian
spellingShingle	Dai, Qian misc Nucleotide Excision Repair misc Ubiquitin Ligase Activity misc Nucleotide Excision Repair Pathway misc Damage Focus misc Histone Ubiquitylation "Cullin 4 makes its mark on chromatin"
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topic_title	"Cullin 4 makes its mark on chromatin" Nucleotide Excision Repair (dpeaa)DE-He213 Ubiquitin Ligase Activity (dpeaa)DE-He213 Nucleotide Excision Repair Pathway (dpeaa)DE-He213 Damage Focus (dpeaa)DE-He213 Histone Ubiquitylation (dpeaa)DE-He213
topic	misc Nucleotide Excision Repair misc Ubiquitin Ligase Activity misc Nucleotide Excision Repair Pathway misc Damage Focus misc Histone Ubiquitylation
topic_unstemmed	misc Nucleotide Excision Repair misc Ubiquitin Ligase Activity misc Nucleotide Excision Repair Pathway misc Damage Focus misc Histone Ubiquitylation
topic_browse	misc Nucleotide Excision Repair misc Ubiquitin Ligase Activity misc Nucleotide Excision Repair Pathway misc Damage Focus misc Histone Ubiquitylation
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title	"Cullin 4 makes its mark on chromatin"
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title_full	"Cullin 4 makes its mark on chromatin"
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title_sort	"cullin 4 makes its mark on chromatin"
title_auth	"Cullin 4 makes its mark on chromatin"
abstract	Abstract Cullin 4 (Cul4), a member of the evolutionally conserved cullin protein family, serves as a scaffold to assemble multisubunit ubiquitin E3 ligase complexes. Cul4 interacts with the Ring finger-containing protein ROC1 through its C-terminal cullin domain and with substrate recruiting subunit(s) through its N-terminus. Previous studies have demonstrated that Cul4 E3 ligase ubiquitylates key regulators in cell cycle control and mediates their degradation through the proteasomal pathway, thus contributing to genome stability. Recent studies from several groups have revealed that Cul4 E3 ligase can target histones for ubiquitylation, and importantly, ubiquitylation of histones may facilitate the cellular response to DNA damage. Therefore, histone ubiquitylation by Cul4 E3 ligase constitutes a novel mechanism through which Cul4 regulates chromatin function and maintains genomic integrity. We outline these studies and suggest that histone ubiquitylation might play important roles in Cul4-regualted chromatin function including the cellular response to DNA damage and heterochromatin gene silencing. © Dai and Wang; licensee BioMed Central Ltd. 2006
abstractGer	Abstract Cullin 4 (Cul4), a member of the evolutionally conserved cullin protein family, serves as a scaffold to assemble multisubunit ubiquitin E3 ligase complexes. Cul4 interacts with the Ring finger-containing protein ROC1 through its C-terminal cullin domain and with substrate recruiting subunit(s) through its N-terminus. Previous studies have demonstrated that Cul4 E3 ligase ubiquitylates key regulators in cell cycle control and mediates their degradation through the proteasomal pathway, thus contributing to genome stability. Recent studies from several groups have revealed that Cul4 E3 ligase can target histones for ubiquitylation, and importantly, ubiquitylation of histones may facilitate the cellular response to DNA damage. Therefore, histone ubiquitylation by Cul4 E3 ligase constitutes a novel mechanism through which Cul4 regulates chromatin function and maintains genomic integrity. We outline these studies and suggest that histone ubiquitylation might play important roles in Cul4-regualted chromatin function including the cellular response to DNA damage and heterochromatin gene silencing. © Dai and Wang; licensee BioMed Central Ltd. 2006
abstract_unstemmed	Abstract Cullin 4 (Cul4), a member of the evolutionally conserved cullin protein family, serves as a scaffold to assemble multisubunit ubiquitin E3 ligase complexes. Cul4 interacts with the Ring finger-containing protein ROC1 through its C-terminal cullin domain and with substrate recruiting subunit(s) through its N-terminus. Previous studies have demonstrated that Cul4 E3 ligase ubiquitylates key regulators in cell cycle control and mediates their degradation through the proteasomal pathway, thus contributing to genome stability. Recent studies from several groups have revealed that Cul4 E3 ligase can target histones for ubiquitylation, and importantly, ubiquitylation of histones may facilitate the cellular response to DNA damage. Therefore, histone ubiquitylation by Cul4 E3 ligase constitutes a novel mechanism through which Cul4 regulates chromatin function and maintains genomic integrity. We outline these studies and suggest that histone ubiquitylation might play important roles in Cul4-regualted chromatin function including the cellular response to DNA damage and heterochromatin gene silencing. © Dai and Wang; licensee BioMed Central Ltd. 2006
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title_short	"Cullin 4 makes its mark on chromatin"
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