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Rab1 Recruitment of p115 into a cis-SNARE Complex: Programming Budding COPII Vesicles for Fusion

Allan, Bernard B., Moyer, Bryan D., Balch, William E.·2000·Science
DOI 10.1126/science.289.5478.444
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Abstract

The guanosine triphosphatase Rab1 regulates the transport of newly synthesized proteins from the endoplasmic reticulum to the Golgi apparatus through interaction with effector molecules, but the molecular mechanisms by which this occurs are unknown. Here, the tethering factor p115 was shown to be a Rab1 effector that binds directly to activated Rab1. Rab1 recruited p115 to coat protein complex II (COPII) vesicles during budding from the endoplasmic reticulum, where it interacted with a select set of COPII vesicle–associated SNAREs (soluble N -ethylmaleimide–sensitive factor attachment protein receptors) to form a cis-SNARE complex that promotes targeting to the Golgi apparatus. We propose that Rab1-regulated assembly of functional effector-SNARE complexes defines a conserved molecular mechanism to coordinate recognition between subcellular compartments.

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Crossref · 10.1126/science.289.5478.444

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  • RUSC2-interacting small G-protein Rab1a regulates trafficking from the Golgi compartment to the plasma membrane.

    “Given the above results, the reported RUSC2 interaction with GM130 (50) and the role of RUSC2-interacting small G-protein Rab1a in regulating trafficking from the Golgi compartment to the plasma membrane (50, 69, 70), we reasoned that RUSC2 may also function in EHD1-dependent EGFR trafficking out of the Golgi compartment.”

    From EHD1 and RUSC2 Control Basal Epidermal Growth Factor Receptor Cell Surface Expression and Recycling (2020) · cites this paper as [69]

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Metadata

Authors
Allan, B. B., Moyer, B. D., & Balch, W. E.
Affiliations
Departments of Cell and Molecular Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2000-07-21
Volume
289
Issue
5478
Pages
444-448
ISSN
  • 0036-8075
  • 1095-9203
DOI
10.1126/science.289.5478.444
Cited by
418
References
2
Language
en

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