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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.
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These data unveil the molecular mechanism of Golgi retention of kAE1 (show OSGEP Proteins) G701D and suggest that disruption of the COPI-kAE1 (show OSGEP Proteins) G701D interaction could be a therapeutic strategy to treat distal renal tubular acidosis caused by this mutant.
ERManI and gamma-COP contribute to a golgi-based quality control module that facilitates the retrieval of captured ERAD substrates back to the endoplasmic reticulum.
The D1 receptor associates with the gamma-subunit of the COPI coatomer (show ARCN1 Proteins) complex. Association between the coatomer (show ARCN1 Proteins) complex and hydrophobic residues within the proximal C-terminus of the D1 receptor may serve an important role in receptor transport.
Results describe the structure of the appendage domain of gamma-COP and show that it has a similar overall fold as the alpha-appendage of AP2 (show GTF3A Proteins).
Data show Trs130 (show TRAPPC9 Proteins) (mTrs130) is a component of an analogous TRAPP complex that this complex is enriched on COPI (Coat Protein (show GOLPH3 Proteins) I (show ANXA2 Proteins))-coated vesicles it specifically activates Rab1 (show RAB1A Proteins).
analysis of differential localization of coatomer (show COPE Proteins) complex isoforms within the Golgi apparatus
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. 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 triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis (By similarity).
coat protein gamma-cop
, coatomer protein complex, subunit gamma 2
, coatomer subunit gamma
, coatomer subunit gamma-1
, gamma-1-coat protein
, gamma-coat protein