TRAPPI tethers COPII vesicles by binding the coat subunit Sec23

Huaqing Cai; Sidney Yu; Shekar Menon; Yiying Cai; Darina Lazarova; Chunmei Fu; Karin Reinisch; Jesse C. Hay; Susan Ferro-Novick

doi:10.1038/nature05527

TRAPPI tethers COPII vesicles by binding the coat subunit Sec23

Huaqing Cai, Sidney Yu, Shekar Menon, Yiying Cai, Darina Lazarova, Chunmei Fu, Karin Reinisch, Jesse C. Hay, Susan Ferro-Novick

Yale University

Research output: Contribution to journal › Article › peer-review

207 Scopus citations

Abstract

The budding of endoplasmic reticulum (ER)-derived vesicles is dependent on the COPII coat complex. Coat assembly is initiated when Sar1-GTP recruits the cargo adaptor complex, Sec23/Sec24, by binding to its GTPase-activating protein (GAP) Sec23 (ref. 2). This leads to the capture of transmembrane cargo by Sec24 (refs 3, 4) before the coat is polymerized by the Sec13/Sec31 complex. The initial interaction of a vesicle with its target membrane is mediated by tethers. We report here that in yeast and mammalian cells the tethering complex TRAPPI (ref. 7) binds to the coat subunit Sec23. This event requires the Bet3 subunit. In vitro studies demonstrate that the interaction between Sec23 and Bet3 targets TRAPPI to COPII vesicles to mediate vesicle tethering. We propose that the binding of TRAPPI to Sec23 marks a coated vesicle for fusion with another COPII vesicle or the Golgi apparatus. An implication of these findings is that the intracellular destination of a transport vesicle may be determined in part by its coat and its associated cargo.

Original language	English
Pages (from-to)	941-944
Number of pages	4
Journal	Nature
Volume	445
Issue number	7130
DOIs	https://doi.org/10.1038/nature05527
State	Published - Feb 22 2007

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title = "TRAPPI tethers COPII vesicles by binding the coat subunit Sec23",

abstract = "The budding of endoplasmic reticulum (ER)-derived vesicles is dependent on the COPII coat complex. Coat assembly is initiated when Sar1-GTP recruits the cargo adaptor complex, Sec23/Sec24, by binding to its GTPase-activating protein (GAP) Sec23 (ref. 2). This leads to the capture of transmembrane cargo by Sec24 (refs 3, 4) before the coat is polymerized by the Sec13/Sec31 complex. The initial interaction of a vesicle with its target membrane is mediated by tethers. We report here that in yeast and mammalian cells the tethering complex TRAPPI (ref. 7) binds to the coat subunit Sec23. This event requires the Bet3 subunit. In vitro studies demonstrate that the interaction between Sec23 and Bet3 targets TRAPPI to COPII vesicles to mediate vesicle tethering. We propose that the binding of TRAPPI to Sec23 marks a coated vesicle for fusion with another COPII vesicle or the Golgi apparatus. An implication of these findings is that the intracellular destination of a transport vesicle may be determined in part by its coat and its associated cargo.",

author = "Huaqing Cai and Sidney Yu and Shekar Menon and Yiying Cai and Darina Lazarova and Chunmei Fu and Karin Reinisch and Hay, {Jesse C.} and Susan Ferro-Novick",

note = "Funding Information: Acknowledgements We thank L. Walker for help in the preparation of the manuscript, Y. Zhang, and K. Mullen for technical assistance. We also thank J. Barrowman for help with the yeast in vitro tethering assay, R. Schekman, C. Kaiser, F. Gorelick and T. Schroer for purified proteins, antibodies, plasmids and strains, and E. Miller for advice on stripping COPII coats from vesicles. This work was supported by the Howard Hughes Medical Institute. Salary support for S.F.-N., H.C., S.Y., S.M. and D.L. was also provided by the Howard Hughes Medical Institute. Work at the University of Montana was supported by an NIH grant to J.C.H. and the NIH-COBRE Center for Structural and Functional Neuroscience.",

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T1 - TRAPPI tethers COPII vesicles by binding the coat subunit Sec23

AU - Cai, Huaqing

AU - Yu, Sidney

AU - Menon, Shekar

AU - Cai, Yiying

AU - Lazarova, Darina

AU - Fu, Chunmei

AU - Reinisch, Karin

AU - Hay, Jesse C.

AU - Ferro-Novick, Susan

N1 - Funding Information: Acknowledgements We thank L. Walker for help in the preparation of the manuscript, Y. Zhang, and K. Mullen for technical assistance. We also thank J. Barrowman for help with the yeast in vitro tethering assay, R. Schekman, C. Kaiser, F. Gorelick and T. Schroer for purified proteins, antibodies, plasmids and strains, and E. Miller for advice on stripping COPII coats from vesicles. This work was supported by the Howard Hughes Medical Institute. Salary support for S.F.-N., H.C., S.Y., S.M. and D.L. was also provided by the Howard Hughes Medical Institute. Work at the University of Montana was supported by an NIH grant to J.C.H. and the NIH-COBRE Center for Structural and Functional Neuroscience.

PY - 2007/2/22

Y1 - 2007/2/22

N2 - The budding of endoplasmic reticulum (ER)-derived vesicles is dependent on the COPII coat complex. Coat assembly is initiated when Sar1-GTP recruits the cargo adaptor complex, Sec23/Sec24, by binding to its GTPase-activating protein (GAP) Sec23 (ref. 2). This leads to the capture of transmembrane cargo by Sec24 (refs 3, 4) before the coat is polymerized by the Sec13/Sec31 complex. The initial interaction of a vesicle with its target membrane is mediated by tethers. We report here that in yeast and mammalian cells the tethering complex TRAPPI (ref. 7) binds to the coat subunit Sec23. This event requires the Bet3 subunit. In vitro studies demonstrate that the interaction between Sec23 and Bet3 targets TRAPPI to COPII vesicles to mediate vesicle tethering. We propose that the binding of TRAPPI to Sec23 marks a coated vesicle for fusion with another COPII vesicle or the Golgi apparatus. An implication of these findings is that the intracellular destination of a transport vesicle may be determined in part by its coat and its associated cargo.

AB - The budding of endoplasmic reticulum (ER)-derived vesicles is dependent on the COPII coat complex. Coat assembly is initiated when Sar1-GTP recruits the cargo adaptor complex, Sec23/Sec24, by binding to its GTPase-activating protein (GAP) Sec23 (ref. 2). This leads to the capture of transmembrane cargo by Sec24 (refs 3, 4) before the coat is polymerized by the Sec13/Sec31 complex. The initial interaction of a vesicle with its target membrane is mediated by tethers. We report here that in yeast and mammalian cells the tethering complex TRAPPI (ref. 7) binds to the coat subunit Sec23. This event requires the Bet3 subunit. In vitro studies demonstrate that the interaction between Sec23 and Bet3 targets TRAPPI to COPII vesicles to mediate vesicle tethering. We propose that the binding of TRAPPI to Sec23 marks a coated vesicle for fusion with another COPII vesicle or the Golgi apparatus. An implication of these findings is that the intracellular destination of a transport vesicle may be determined in part by its coat and its associated cargo.

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VL - 445

SP - 941

EP - 944

JO - Nature

JF - Nature

IS - 7130

ER -

TRAPPI tethers COPII vesicles by binding the coat subunit Sec23

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