ARFGAP1 plays a central role in coupling COPI cargo sorting with vesicle formation.
Abstract
Examining how key components of coat protein I (COPI) transport participate in cargo
sorting, we find that, instead of ADP ribosylation factor 1 (ARF1), its GTPase-activating
protein (GAP) plays a direct role in promoting the binding of cargo proteins by coatomer
(the core COPI complex). Activated ARF1 binds selectively to SNARE cargo proteins,
with this binding likely to represent at least a mechanism by which activated ARF1
is stabilized on Golgi membrane to propagate its effector functions. We also find
that the GAP catalytic activity plays a critical role in the formation of COPI vesicles
from Golgi membrane, in contrast to the prevailing view that this activity antagonizes
vesicle formation. Together, these findings indicate that GAP plays a central role
in coupling cargo sorting and vesicle formation, with implications for simplifying
models to describe how these two processes are coupled during COPI transport.
Type
Journal articleSubject
ADP-Ribosylation Factor 1ADP-Ribosylation Factors
COP-Coated Vesicles
Coat Protein Complex I
Coatomer Protein
GTPase-Activating Proteins
Golgi Apparatus
Guanosine Triphosphate
Intracellular Membranes
Mutation
Protein Binding
Protein Transport
Recombinant Proteins
SNARE Proteins
Transport Vesicles
Vesicular Transport Proteins
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https://hdl.handle.net/10161/10775Published Version (Please cite this version)
10.1083/jcb.200404008Publication Info
Lee, SY; Yang, JS; Hong, W; Premont, RT; & Hsu, VW (2005). ARFGAP1 plays a central role in coupling COPI cargo sorting with vesicle formation.
J Cell Biol, 168(2). pp. 281-290. 10.1083/jcb.200404008. Retrieved from https://hdl.handle.net/10161/10775.This is constructed from limited available data and may be imprecise. To cite this
article, please review & use the official citation provided by the journal.
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Show full item recordScholars@Duke
Richard Thomas Premont
Associate Professor in Medicine
Critical physiological events throughout the body are controlled by extracellular
signals from neurotransmitters and hormones acting on cell surface receptors. Receptors
transduce these signals to alter intracellular metabolism and cellular responsiveness
through heterotrimeric G protein/second messenger pathways or through small GTP-binding
protein/protein kinase cascades. The mechanisms that control the responsiveness of
target organ G protein-coupled receptors include receptor ph

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