4j82: Difference between revisions
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==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/INSI2_HUMAN INSI2_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. Seems to regulate the ubiquitin-mediated proteasomal degradation of HMGCR.<ref>PMID:12242332</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/INSI2_HUMAN INSI2_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. Seems to regulate the ubiquitin-mediated proteasomal degradation of HMGCR.<ref>PMID:12242332</ref> <ref>PMID:16606821</ref> | ||
==About this Structure== | ==About this Structure== | ||
Revision as of 22:25, 17 April 2013
Crystal structure of beta'-COP/Insig-2 complexCrystal structure of beta'-COP/Insig-2 complex
Template:ABSTRACT PUBMED 23481256
FunctionFunction
[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.[1] [INSI2_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. Seems to regulate the ubiquitin-mediated proteasomal degradation of HMGCR.[2] [3]
About this StructureAbout this Structure
4j82 is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Gabriely G, Kama R, Gerst JE. Involvement of specific COPI subunits in protein sorting from the late endosome to the vacuole in yeast. Mol Cell Biol. 2007 Jan;27(2):526-40. Epub 2006 Nov 13. PMID:17101773 doi:MCB.00577-06
- ↑ Yabe D, Brown MS, Goldstein JL. Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins. Proc Natl Acad Sci U S A. 2002 Oct 1;99(20):12753-8. Epub 2002 Sep 19. PMID:12242332 doi:10.1073/pnas.162488899
- ↑ Gong Y, Lee JN, Brown MS, Goldstein JL, Ye J. Juxtamembranous aspartic acid in Insig-1 and Insig-2 is required for cholesterol homeostasis. Proc Natl Acad Sci U S A. 2006 Apr 18;103(16):6154-9. Epub 2006 Apr 10. PMID:16606821 doi:0601923103