4j81: Difference between revisions
No edit summary |
No edit summary |
||
Line 4: | Line 4: | ||
==Function== | ==Function== | ||
[[http://www.uniprot.org/uniprot/COPB2_YEAST COPB2_YEAST]] 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.<ref>PMID:17101773</ref> [[http://www.uniprot.org/uniprot/INSI1_HUMAN INSI1_HUMAN]] Mediates feedback control of cholesterol synthesis by controlling SCAP and HMGCR. Functions by blocking the processing of sterol regulatory element-binding proteins (SREBPs). Capable of retaining the SCAP-SREBF2 complex in the ER thus preventing it from escorting SREBPs to the Golgi. Initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligase, AMFR/gp78. May play a role in growth and differentiation of tissues involved in metabolic control. May play a regulatory role during G0/G1 transition of cell growth.<ref>PMID:12202038</ref><ref>PMID:12535518</ref><ref>PMID:16168377</ref><ref>PMID:16399501</ref><ref>PMID:16606821</ref> | [[http://www.uniprot.org/uniprot/COPB2_YEAST COPB2_YEAST]] 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.<ref>PMID:17101773</ref> [[http://www.uniprot.org/uniprot/INSI1_HUMAN INSI1_HUMAN]] Mediates feedback control of cholesterol synthesis by controlling SCAP and HMGCR. Functions by blocking the processing of sterol regulatory element-binding proteins (SREBPs). Capable of retaining the SCAP-SREBF2 complex in the ER thus preventing it from escorting SREBPs to the Golgi. Initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligase, AMFR/gp78. May play a role in growth and differentiation of tissues involved in metabolic control. May play a regulatory role during G0/G1 transition of cell growth.<ref>PMID:12202038</ref> <ref>PMID:12535518</ref> <ref>PMID:16168377</ref> <ref>PMID:16399501</ref> <ref>PMID:16606821</ref> | ||
==About this Structure== | ==About this Structure== |