ARFGAP1 plays a central role in coupling COPI cargo sorting with vesicle formation.
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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.
SubjectADP-Ribosylation Factor 1
Coat Protein Complex I
Vesicular Transport Proteins
Published Version (Please cite this version)10.1083/jcb.200404008
Publication InfoHong, W; Hsu, VW; Lee, SY; Premont, Richard Thomas; & Yang, J-S (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.
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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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