Rewiring a Rab regulatory network reveals a possible inhibitory role for the vesicle tether, Uso1
Ypt1 and Sec4 are essential Rab GTPases that control the early and late stages of the yeast secretory pathway, respectively. A chimera consisting of Ypt1 with the switch I domain of Sec4, Ypt1-SW1Sec4, is efficiently activated in vitro by the Sec4 exchange factor, Sec2. This should lead to its ectop...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Yuan, Hua [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Proceedings of the National Academy of Sciences of the United States of America - Washington, DC : NAS, 1877, 114(2017), 41, Seite E8637 |
|---|---|
| Übergeordnetes Werk: |
volume:114 ; year:2017 ; number:41 ; pages:E8637 |
| Links: |
|---|
| DOI / URN: |
10.1073/pnas.1708394114 |
|---|
| Katalog-ID: |
OLC1999832868 |
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| 520 | |a Ypt1 and Sec4 are essential Rab GTPases that control the early and late stages of the yeast secretory pathway, respectively. A chimera consisting of Ypt1 with the switch I domain of Sec4, Ypt1-SW1Sec4, is efficiently activated in vitro by the Sec4 exchange factor, Sec2. This should lead to its ectopic activation in vivo and thereby disrupt membrane traffic. Nonetheless early studies found that yeast expressing Ypt1-SW1Sec4 as the sole copy of YPT1 exhibit no growth defect. To resolve this conundrum, we have analyzed yeast expressing various levels of Ypt1-SW1Sec4. We show that even normal expression of Ypt1-SW1Sec4 leads to kinetic transport defects at a late stage of the pathway, with secretory vesicles accumulating near exocytic sites. Higher levels are toxic. Toxicity is suppressed by truncation of Uso1, a vesicle tether required for endoplasmic reticulum-Golgi traffic. The globular head of Uso1 binds to Ypt1 and its coiled-coil tail binds to the Golgi-associated SNARE, Sed5. We propose that when Uso1 is inappropriately recruited to secretory vesicles by Ypt1-SW1Sec4, the extended coiled-coil tail blocks docking to the plasma membrane. This putative inhibitory function could serve to increase the fidelity of vesicle docking. | ||
| 650 | 4 | |a Guanosine triphosphatase | |
| 650 | 4 | |a Physiological aspects | |
| 650 | 4 | |a Golgi apparatus | |
| 650 | 4 | |a Biocompatibility | |
| 650 | 4 | |a Membranes | |
| 650 | 4 | |a In vivo methods and tests | |
| 650 | 4 | |a Coiling | |
| 650 | 4 | |a Rewiring | |
| 650 | 4 | |a Membrane trafficking | |
| 650 | 4 | |a Auditory defects | |
| 650 | 4 | |a Docking | |
| 650 | 4 | |a Toxicity | |
| 650 | 4 | |a SNAP receptors | |
| 650 | 4 | |a Traffic | |
| 650 | 4 | |a Yeast | |
| 650 | 4 | |a Eukaryotes | |
| 650 | 4 | |a Endoplasmic reticulum | |
| 650 | 4 | |a Secretory vesicles | |
| 650 | 4 | |a Cellular biology | |
| 650 | 4 | |a Proteins | |
| 650 | 4 | |a Vesicles | |
| 700 | 1 | |a Davis, Saralin |4 oth | |
| 700 | 1 | |a Ferro-Novick, Susan |4 oth | |
| 700 | 1 | |a Novick, Peter |4 oth | |
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10.1073/pnas.1708394114 doi PQ20171228 (DE-627)OLC1999832868 (DE-599)GBVOLC1999832868 (PRQ)g1164-a32f0723b36da5fca42343af7ff796a874df546ad118afea0ec3e0c559fadf0 (KEY)0583363920170000114004108637rewiringarabregulatorynetworkrevealsapossibleinhib DE-627 ger DE-627 rakwb eng 500 DE-101 570 AVZ LING fid BIODIV fid Yuan, Hua verfasserin aut Rewiring a Rab regulatory network reveals a possible inhibitory role for the vesicle tether, Uso1 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Ypt1 and Sec4 are essential Rab GTPases that control the early and late stages of the yeast secretory pathway, respectively. A chimera consisting of Ypt1 with the switch I domain of Sec4, Ypt1-SW1Sec4, is efficiently activated in vitro by the Sec4 exchange factor, Sec2. This should lead to its ectopic activation in vivo and thereby disrupt membrane traffic. Nonetheless early studies found that yeast expressing Ypt1-SW1Sec4 as the sole copy of YPT1 exhibit no growth defect. To resolve this conundrum, we have analyzed yeast expressing various levels of Ypt1-SW1Sec4. We show that even normal expression of Ypt1-SW1Sec4 leads to kinetic transport defects at a late stage of the pathway, with secretory vesicles accumulating near exocytic sites. Higher levels are toxic. Toxicity is suppressed by truncation of Uso1, a vesicle tether required for endoplasmic reticulum-Golgi traffic. The globular head of Uso1 binds to Ypt1 and its coiled-coil tail binds to the Golgi-associated SNARE, Sed5. We propose that when Uso1 is inappropriately recruited to secretory vesicles by Ypt1-SW1Sec4, the extended coiled-coil tail blocks docking to the plasma membrane. This putative inhibitory function could serve to increase the fidelity of vesicle docking. Guanosine triphosphatase Physiological aspects Golgi apparatus Biocompatibility Membranes In vivo methods and tests Coiling Rewiring Membrane trafficking Auditory defects Docking Toxicity SNAP receptors Traffic Yeast Eukaryotes Endoplasmic reticulum Secretory vesicles Cellular biology Proteins Vesicles Davis, Saralin oth Ferro-Novick, Susan oth Novick, Peter oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 114(2017), 41, Seite E8637 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:114 year:2017 number:41 pages:E8637 http://dx.doi.org/10.1073/pnas.1708394114 Volltext https://search.proquest.com/docview/1970169912 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 114 2017 41 E8637 |
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10.1073/pnas.1708394114 doi PQ20171228 (DE-627)OLC1999832868 (DE-599)GBVOLC1999832868 (PRQ)g1164-a32f0723b36da5fca42343af7ff796a874df546ad118afea0ec3e0c559fadf0 (KEY)0583363920170000114004108637rewiringarabregulatorynetworkrevealsapossibleinhib DE-627 ger DE-627 rakwb eng 500 DE-101 570 AVZ LING fid BIODIV fid Yuan, Hua verfasserin aut Rewiring a Rab regulatory network reveals a possible inhibitory role for the vesicle tether, Uso1 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Ypt1 and Sec4 are essential Rab GTPases that control the early and late stages of the yeast secretory pathway, respectively. A chimera consisting of Ypt1 with the switch I domain of Sec4, Ypt1-SW1Sec4, is efficiently activated in vitro by the Sec4 exchange factor, Sec2. This should lead to its ectopic activation in vivo and thereby disrupt membrane traffic. Nonetheless early studies found that yeast expressing Ypt1-SW1Sec4 as the sole copy of YPT1 exhibit no growth defect. To resolve this conundrum, we have analyzed yeast expressing various levels of Ypt1-SW1Sec4. We show that even normal expression of Ypt1-SW1Sec4 leads to kinetic transport defects at a late stage of the pathway, with secretory vesicles accumulating near exocytic sites. Higher levels are toxic. Toxicity is suppressed by truncation of Uso1, a vesicle tether required for endoplasmic reticulum-Golgi traffic. The globular head of Uso1 binds to Ypt1 and its coiled-coil tail binds to the Golgi-associated SNARE, Sed5. We propose that when Uso1 is inappropriately recruited to secretory vesicles by Ypt1-SW1Sec4, the extended coiled-coil tail blocks docking to the plasma membrane. This putative inhibitory function could serve to increase the fidelity of vesicle docking. Guanosine triphosphatase Physiological aspects Golgi apparatus Biocompatibility Membranes In vivo methods and tests Coiling Rewiring Membrane trafficking Auditory defects Docking Toxicity SNAP receptors Traffic Yeast Eukaryotes Endoplasmic reticulum Secretory vesicles Cellular biology Proteins Vesicles Davis, Saralin oth Ferro-Novick, Susan oth Novick, Peter oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 114(2017), 41, Seite E8637 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:114 year:2017 number:41 pages:E8637 http://dx.doi.org/10.1073/pnas.1708394114 Volltext https://search.proquest.com/docview/1970169912 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 114 2017 41 E8637 |
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10.1073/pnas.1708394114 doi PQ20171228 (DE-627)OLC1999832868 (DE-599)GBVOLC1999832868 (PRQ)g1164-a32f0723b36da5fca42343af7ff796a874df546ad118afea0ec3e0c559fadf0 (KEY)0583363920170000114004108637rewiringarabregulatorynetworkrevealsapossibleinhib DE-627 ger DE-627 rakwb eng 500 DE-101 570 AVZ LING fid BIODIV fid Yuan, Hua verfasserin aut Rewiring a Rab regulatory network reveals a possible inhibitory role for the vesicle tether, Uso1 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Ypt1 and Sec4 are essential Rab GTPases that control the early and late stages of the yeast secretory pathway, respectively. A chimera consisting of Ypt1 with the switch I domain of Sec4, Ypt1-SW1Sec4, is efficiently activated in vitro by the Sec4 exchange factor, Sec2. This should lead to its ectopic activation in vivo and thereby disrupt membrane traffic. Nonetheless early studies found that yeast expressing Ypt1-SW1Sec4 as the sole copy of YPT1 exhibit no growth defect. To resolve this conundrum, we have analyzed yeast expressing various levels of Ypt1-SW1Sec4. We show that even normal expression of Ypt1-SW1Sec4 leads to kinetic transport defects at a late stage of the pathway, with secretory vesicles accumulating near exocytic sites. Higher levels are toxic. Toxicity is suppressed by truncation of Uso1, a vesicle tether required for endoplasmic reticulum-Golgi traffic. The globular head of Uso1 binds to Ypt1 and its coiled-coil tail binds to the Golgi-associated SNARE, Sed5. We propose that when Uso1 is inappropriately recruited to secretory vesicles by Ypt1-SW1Sec4, the extended coiled-coil tail blocks docking to the plasma membrane. This putative inhibitory function could serve to increase the fidelity of vesicle docking. Guanosine triphosphatase Physiological aspects Golgi apparatus Biocompatibility Membranes In vivo methods and tests Coiling Rewiring Membrane trafficking Auditory defects Docking Toxicity SNAP receptors Traffic Yeast Eukaryotes Endoplasmic reticulum Secretory vesicles Cellular biology Proteins Vesicles Davis, Saralin oth Ferro-Novick, Susan oth Novick, Peter oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 114(2017), 41, Seite E8637 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:114 year:2017 number:41 pages:E8637 http://dx.doi.org/10.1073/pnas.1708394114 Volltext https://search.proquest.com/docview/1970169912 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 114 2017 41 E8637 |
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10.1073/pnas.1708394114 doi PQ20171228 (DE-627)OLC1999832868 (DE-599)GBVOLC1999832868 (PRQ)g1164-a32f0723b36da5fca42343af7ff796a874df546ad118afea0ec3e0c559fadf0 (KEY)0583363920170000114004108637rewiringarabregulatorynetworkrevealsapossibleinhib DE-627 ger DE-627 rakwb eng 500 DE-101 570 AVZ LING fid BIODIV fid Yuan, Hua verfasserin aut Rewiring a Rab regulatory network reveals a possible inhibitory role for the vesicle tether, Uso1 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Ypt1 and Sec4 are essential Rab GTPases that control the early and late stages of the yeast secretory pathway, respectively. A chimera consisting of Ypt1 with the switch I domain of Sec4, Ypt1-SW1Sec4, is efficiently activated in vitro by the Sec4 exchange factor, Sec2. This should lead to its ectopic activation in vivo and thereby disrupt membrane traffic. Nonetheless early studies found that yeast expressing Ypt1-SW1Sec4 as the sole copy of YPT1 exhibit no growth defect. To resolve this conundrum, we have analyzed yeast expressing various levels of Ypt1-SW1Sec4. We show that even normal expression of Ypt1-SW1Sec4 leads to kinetic transport defects at a late stage of the pathway, with secretory vesicles accumulating near exocytic sites. Higher levels are toxic. Toxicity is suppressed by truncation of Uso1, a vesicle tether required for endoplasmic reticulum-Golgi traffic. The globular head of Uso1 binds to Ypt1 and its coiled-coil tail binds to the Golgi-associated SNARE, Sed5. We propose that when Uso1 is inappropriately recruited to secretory vesicles by Ypt1-SW1Sec4, the extended coiled-coil tail blocks docking to the plasma membrane. This putative inhibitory function could serve to increase the fidelity of vesicle docking. Guanosine triphosphatase Physiological aspects Golgi apparatus Biocompatibility Membranes In vivo methods and tests Coiling Rewiring Membrane trafficking Auditory defects Docking Toxicity SNAP receptors Traffic Yeast Eukaryotes Endoplasmic reticulum Secretory vesicles Cellular biology Proteins Vesicles Davis, Saralin oth Ferro-Novick, Susan oth Novick, Peter oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 114(2017), 41, Seite E8637 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:114 year:2017 number:41 pages:E8637 http://dx.doi.org/10.1073/pnas.1708394114 Volltext https://search.proquest.com/docview/1970169912 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 114 2017 41 E8637 |
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10.1073/pnas.1708394114 doi PQ20171228 (DE-627)OLC1999832868 (DE-599)GBVOLC1999832868 (PRQ)g1164-a32f0723b36da5fca42343af7ff796a874df546ad118afea0ec3e0c559fadf0 (KEY)0583363920170000114004108637rewiringarabregulatorynetworkrevealsapossibleinhib DE-627 ger DE-627 rakwb eng 500 DE-101 570 AVZ LING fid BIODIV fid Yuan, Hua verfasserin aut Rewiring a Rab regulatory network reveals a possible inhibitory role for the vesicle tether, Uso1 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Ypt1 and Sec4 are essential Rab GTPases that control the early and late stages of the yeast secretory pathway, respectively. A chimera consisting of Ypt1 with the switch I domain of Sec4, Ypt1-SW1Sec4, is efficiently activated in vitro by the Sec4 exchange factor, Sec2. This should lead to its ectopic activation in vivo and thereby disrupt membrane traffic. Nonetheless early studies found that yeast expressing Ypt1-SW1Sec4 as the sole copy of YPT1 exhibit no growth defect. To resolve this conundrum, we have analyzed yeast expressing various levels of Ypt1-SW1Sec4. We show that even normal expression of Ypt1-SW1Sec4 leads to kinetic transport defects at a late stage of the pathway, with secretory vesicles accumulating near exocytic sites. Higher levels are toxic. Toxicity is suppressed by truncation of Uso1, a vesicle tether required for endoplasmic reticulum-Golgi traffic. The globular head of Uso1 binds to Ypt1 and its coiled-coil tail binds to the Golgi-associated SNARE, Sed5. We propose that when Uso1 is inappropriately recruited to secretory vesicles by Ypt1-SW1Sec4, the extended coiled-coil tail blocks docking to the plasma membrane. This putative inhibitory function could serve to increase the fidelity of vesicle docking. Guanosine triphosphatase Physiological aspects Golgi apparatus Biocompatibility Membranes In vivo methods and tests Coiling Rewiring Membrane trafficking Auditory defects Docking Toxicity SNAP receptors Traffic Yeast Eukaryotes Endoplasmic reticulum Secretory vesicles Cellular biology Proteins Vesicles Davis, Saralin oth Ferro-Novick, Susan oth Novick, Peter oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 114(2017), 41, Seite E8637 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:114 year:2017 number:41 pages:E8637 http://dx.doi.org/10.1073/pnas.1708394114 Volltext https://search.proquest.com/docview/1970169912 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 114 2017 41 E8637 |
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rewiring a rab regulatory network reveals a possible inhibitory role for the vesicle tether, uso1 |
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Rewiring a Rab regulatory network reveals a possible inhibitory role for the vesicle tether, Uso1 |
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Ypt1 and Sec4 are essential Rab GTPases that control the early and late stages of the yeast secretory pathway, respectively. A chimera consisting of Ypt1 with the switch I domain of Sec4, Ypt1-SW1Sec4, is efficiently activated in vitro by the Sec4 exchange factor, Sec2. This should lead to its ectopic activation in vivo and thereby disrupt membrane traffic. Nonetheless early studies found that yeast expressing Ypt1-SW1Sec4 as the sole copy of YPT1 exhibit no growth defect. To resolve this conundrum, we have analyzed yeast expressing various levels of Ypt1-SW1Sec4. We show that even normal expression of Ypt1-SW1Sec4 leads to kinetic transport defects at a late stage of the pathway, with secretory vesicles accumulating near exocytic sites. Higher levels are toxic. Toxicity is suppressed by truncation of Uso1, a vesicle tether required for endoplasmic reticulum-Golgi traffic. The globular head of Uso1 binds to Ypt1 and its coiled-coil tail binds to the Golgi-associated SNARE, Sed5. We propose that when Uso1 is inappropriately recruited to secretory vesicles by Ypt1-SW1Sec4, the extended coiled-coil tail blocks docking to the plasma membrane. This putative inhibitory function could serve to increase the fidelity of vesicle docking. |
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Ypt1 and Sec4 are essential Rab GTPases that control the early and late stages of the yeast secretory pathway, respectively. A chimera consisting of Ypt1 with the switch I domain of Sec4, Ypt1-SW1Sec4, is efficiently activated in vitro by the Sec4 exchange factor, Sec2. This should lead to its ectopic activation in vivo and thereby disrupt membrane traffic. Nonetheless early studies found that yeast expressing Ypt1-SW1Sec4 as the sole copy of YPT1 exhibit no growth defect. To resolve this conundrum, we have analyzed yeast expressing various levels of Ypt1-SW1Sec4. We show that even normal expression of Ypt1-SW1Sec4 leads to kinetic transport defects at a late stage of the pathway, with secretory vesicles accumulating near exocytic sites. Higher levels are toxic. Toxicity is suppressed by truncation of Uso1, a vesicle tether required for endoplasmic reticulum-Golgi traffic. The globular head of Uso1 binds to Ypt1 and its coiled-coil tail binds to the Golgi-associated SNARE, Sed5. We propose that when Uso1 is inappropriately recruited to secretory vesicles by Ypt1-SW1Sec4, the extended coiled-coil tail blocks docking to the plasma membrane. This putative inhibitory function could serve to increase the fidelity of vesicle docking. |
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Ypt1 and Sec4 are essential Rab GTPases that control the early and late stages of the yeast secretory pathway, respectively. A chimera consisting of Ypt1 with the switch I domain of Sec4, Ypt1-SW1Sec4, is efficiently activated in vitro by the Sec4 exchange factor, Sec2. This should lead to its ectopic activation in vivo and thereby disrupt membrane traffic. Nonetheless early studies found that yeast expressing Ypt1-SW1Sec4 as the sole copy of YPT1 exhibit no growth defect. To resolve this conundrum, we have analyzed yeast expressing various levels of Ypt1-SW1Sec4. We show that even normal expression of Ypt1-SW1Sec4 leads to kinetic transport defects at a late stage of the pathway, with secretory vesicles accumulating near exocytic sites. Higher levels are toxic. Toxicity is suppressed by truncation of Uso1, a vesicle tether required for endoplasmic reticulum-Golgi traffic. The globular head of Uso1 binds to Ypt1 and its coiled-coil tail binds to the Golgi-associated SNARE, Sed5. We propose that when Uso1 is inappropriately recruited to secretory vesicles by Ypt1-SW1Sec4, the extended coiled-coil tail blocks docking to the plasma membrane. This putative inhibitory function could serve to increase the fidelity of vesicle docking. |
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