COPB2

The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).

This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner.

Belongs to the WD repeat COPB2 family.

• Cytoplasm
• Cytosol
• Golgi apparatus membrane
• Peripheral membrane protein
• Cytoplasmic side
• Cytoplasmic vesicle
• COPI-coated vesicle membrane
• Peripheral membrane protein
• Cytoplasmic side
• The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it (By similarity). Shows only a slight preference for the cis-Golgi apparatus (<55%), compared with the trans-Golgi (>45%).

Coatomer subunit beta', Beta'-coat protein, p102, Beta'-COP, Copb2

• swissprot:O35142

Proteins

Oncology

102551Da