COPB1
Description
The COPB1 (COPI coat complex subunit beta 1) is a protein-coding gene located on chromosome 11.
Coatomer subunit beta is a protein that in humans is encoded by the COPB1 gene.
== See also == COPI coatomer, a protein complex
== References ==
== Further reading ==
== External links == Human COPB1 genome location and COPB1 gene details page in the UCSC Genome Browser.
COPB1, also known as Beta-coat protein, is a subunit of the coatomer complex. The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, mediating biosynthetic protein transport from the ER to the Golgi and the trans Golgi network. It is essential for budding from Golgi membranes and for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, coatomer recruitment to membranes requires ADP-ribosylation factors (ARFs), small GTP-binding proteins. COPB1 influences Golgi structural integrity, LDL receptor processing, activity, and endocytic recycling. It facilitates the transport of kappa-type opioid receptor mRNAs into axons and enhances their translation. COPB1 is required for limiting lipid storage in lipid droplets and plays a role in lipid homeostasis by regulating perilipin family members PLIN2 and PLIN3 at the lipid droplet surface, promoting PNPLA2 association with lipid droplets for lipolysis. COPB1 is involved in Golgi disassembly and reassembly during the cell cycle and in autophagy by regulating early endosome function. It contributes to organellar compartmentalization of secretory compartments, including the ER-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN), and recycling endosomes, and to CAV1 biosynthetic transport. COPB1 promotes degradation of Nef cellular targets CD4 and MHC class I antigens by facilitating their trafficking to degradative compartments.
COPB1 is also known as BARMACS, COPB.
