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17.5 : Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.

Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling vesicular traffic by identifying compartments and determining the time and place of coat assembly. The adaptor protein binds transmembrane receptors involved in cargo capture, thus indirectly playing a role in cargo selectivity. Adaptor proteins are specific for the type of cargo receptor. Hence, distinct adaptor proteins are involved in the budding of clathrin-coated vesicles from different membranes.

Vesicular traffic is a tightly regulated process. So, coat proteins assemble and initiate bending the membrane budding of the vesicle only when vesicle formation is initiated locally at the membrane. Different small GTPases control the assembly of coat proteins by switching between GTP and GDP-bound states. ARF, a monomeric GTPase, regulates COPI and clathrin coat assembly in the Golgi membrane, while another small GTPase, Sar1 protein, regulates COPII coat assembly in the ER.

Tags
Coat AssemblyGTPasesVesiclesCoat Protein SubunitsTransport VesiclesCargo SelectionPhosphatidylinositol Phosphates PIPsGTP binding ProteinsAdaptor ProteinsMembraneCargo CaptureCargo SelectivityClathrin coated VesiclesVesicular TrafficCoat ProteinsMembrane BuddingSmall GTPasesARF ProteinGolgi MembraneSar1 ProteinER endoplasmic Reticulum

From Chapter 17:

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17.5 : Coat Assembly and GTPases

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17.11 : ER Retrieval Pathway

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17.12 : Golgi Apparatus

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