Coatomer proteins are involved in regulating transport between the endoplasmic reticulum (ER) and the Golgi complex and in intra-Golgi transport. There exist two coatomer-protein mechanisms (COP I and COP II) and although they have mechanistic parallels, they are molecularly distinct. The COP I coat is comprised of seven subunits (alpha-, beta-, beta'-, gamma-, delta-, epsilon-, and zeta-COP) in a complex called coatomer. Assembly of the coatomer (COP I) onto non-clathrin coated vesicles is regulated by ADP-ribosylation factor (ARF). Vesicle formation, budding, fusion, and disassembly is dependent on GDP-GTP exchange, COP I, and ARF. COP I has been shown to facilitate retrograde intracellular transport from the ER to the Golgi complex. By contrast, COP II facilitates anterograde transport between these subcellular organelles. COP II has been shown to be independently and selectively recruited to the ER relative to COP I subunits.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/1000. Detects a band of approximately 110 kDa.
1/2000. Golgi localization of beta-COP is sensitive to treatment with brefeldin A or ATP depletion.
Use at an assay dependent concentration. PubMed: 18556652
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. Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte surface triglyceride lipase (PNPLA2) with the lipid droplet to mediate lipolysis (By similarity). Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1. Promotes degradation of Nef cellular targets CD4 and MHC class I antigens by facilitating their trafficking to degradative compartments.
Contains 6 HEAT repeats.
Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8.
Cytoplasm. Golgi apparatus membrane. Cytoplasmic vesicle > COPI-coated vesicle membrane. Cell membrane. Endoplasmic reticulum-Golgi intermediate compartment. The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Proteolytic cleavage by CAPN8 triggers translocation from Golgi to cytoplasm (By similarity). Found in perinuclear vesicular-tubular clusters (VTCs) and in the Golgi region where associated with vesicles, buds and rims of the Golgi stack (By similarity). Occasionally present at the trans-side of Golgi, but mainly present at the cis-Golgi side in transitional areas (TA), on so-called peripheral elements (PE) consisting of tubules and vesicles located between the cup-shaped transitional elements (TE) of the rough endoplasmic reticulum (RER) and the cis-most Golgi cisternae (By similarity). Present in cytoplasm, not associated with visible coats or membranes, with a minor fraction present on small clusters of tubules and vesicles (By similarity). Some association with high-density and low-density microsomes and mitochondria/nuclei fraction (By similarity). Very little found in plasma membrane fraction.