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

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...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2000-07, Vol.289 (5478), p.444-448
Main Authors: Allan, Bernard B., Moyer, Bryan D., Balch, William E.
Format: Article
Language:English
Subjects:
Animals
Antibodies
Biological and medical sciences
Biological Transport
Budding
Carrier Proteins - metabolism
Cell physiology
Cytosol
Endoplasmic Reticulum - metabolism
Fundamental and applied biological sciences. Psychology
Golgi apparatus
Golgi Apparatus - metabolism
Golgi Matrix Proteins
Hepatitis delta virus
Ice
Intracellular Membranes - metabolism
Liver
Membrane and intracellular transports
Membrane Fusion
Membrane Glycoproteins
Membrane Proteins - metabolism
Molecular and cellular biology
Molecules
Mutation
Organelles - metabolism
p115 protein
Phosphoproteins - metabolism
rab1 GTP-Binding Proteins - metabolism
Rab1 protein
Rats
Recombinant Fusion Proteins - metabolism
Saccharomyces cerevisiae Proteins
SNARE complex
SNARE Proteins
Space life sciences
Vesicular Transport Proteins
Viral Envelope Proteins - metabolism
Yeasts
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Summary: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.289.5478.444