Charged multivesicular body protein
From Proteopedia
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== Function == | == Function == | ||
| - | '''Charged multivesicular body protein''' (CHMP)s are part of '''E'''ndosomal '''S'''orting '''C'''omplex '''R'''equired for '''T'''ransport ('''ESCRT''') together with the [[Vacuolar protein sorting-associated protein]]s that performs the topologically unique membrane bending and scission reaction away from the cytoplasm. This process is required for the multivesicular body (MVP) pathway, cytokinesis and HIV budding. There are five distinct ESCRT complexes (0,I,II,III,Vps4) with distinct functions<ref>PMID:22361144</ref>. CHMPs are part of the ESCRT-III complex. | + | '''Charged multivesicular body protein''' (CHMP)s are part of '''E'''ndosomal '''S'''orting '''C'''omplex '''R'''equired for '''T'''ransport ('''ESCRT''') together with the [[Vacuolar protein sorting-associated protein]]s that performs the topologically unique membrane bending and scission reaction away from the cytoplasm. This process is required for the multivesicular body (MVP) pathway, cytokinesis and HIV budding. There are five distinct ESCRT complexes (0,I,II,III,Vps4) with distinct functions<ref>PMID:22361144</ref>. CHMPs are part of the ESCRT-III complex. |
| - | *'''CHMP1A''' and ''' | + | *'''CHMP1A''' and '''CHMP1B''' are required for bodies containing plastid material during autophagy into the cytoplasm <ref>PMID:25649438</ref>.<br /> |
| - | *'''CHMP2B''' | + | *'''CHMP2B''' polymerization scaffolds membranes as part of outward membrane deformation<ref>PMID:21926173</ref>.<br /> |
| + | *'''CHMP3''' sorts transmembrane proteins into lysosomes/vacuoles via the multivesicular body pathway. . | ||
*'''CHMP4B''' circular filament arrays can promote or stabilize negative membrane curvature and outward budding. | *'''CHMP4B''' circular filament arrays can promote or stabilize negative membrane curvature and outward budding. | ||
*'''CHMP5''' has possibly a regulatory role on apoptosis-associated genes. | *'''CHMP5''' has possibly a regulatory role on apoptosis-associated genes. | ||
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== Structural highlights == | == Structural highlights == | ||
| - | The ampiphatic CHMP5 creates a hydrophobic binding collar that includes 6 invariant Leu residues which make hydrophobic interactions with the vacuolar protein sorting-associated protein Vta1 homolog. A strong charge complementarity is formed between CHMP5 negative surface which includes 13 Asp and Glu residues and 11 basic residues on the vacuolar protein sorting-associated protein Vta1 homolog binding surface<ref>PMID:23105106</ref>. | + | The ampiphatic CHMP5 creates a hydrophobic binding collar that includes <scene name='80/803956/Cv/3'>6 invariant Leu residues</scene> which make <scene name='80/803956/Cv/4'>hydrophobic interactions with the vacuolar protein sorting-associated protein Vta1 homolog</scene>. A <scene name='80/803956/Cv/5'>strong charge complementarity</scene> is formed between CHMP5 negative surface which includes 13 Asp and Glu residues and 11 basic residues on the vacuolar protein sorting-associated protein Vta1 homolog binding surface<ref>PMID:23105106</ref>. |
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==3D structures of charged multivesicular body protein== | ==3D structures of charged multivesicular body protein== | ||
| + | [[Charged multivesicular body protein 3D structures]] | ||
| - | + | </StructureSection> | |
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== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ Schmidt O, Teis D. The ESCRT machinery. Curr Biol. 2012 Feb 21;22(4):R116-20. doi: 10.1016/j.cub.2012.01.028. PMID:22361144 doi:http://dx.doi.org/10.1016/j.cub.2012.01.028
- ↑ Spitzer C, Li F, Buono R, Roschzttardtz H, Chung T, Zhang M, Osteryoung KW, Vierstra RD, Otegui MS. The endosomal protein CHARGED MULTIVESICULAR BODY PROTEIN1 regulates the autophagic turnover of plastids in Arabidopsis. Plant Cell. 2015 Feb;27(2):391-402. doi: 10.1105/tpc.114.135939. Epub 2015 Feb 3. PMID:25649438 doi:http://dx.doi.org/10.1105/tpc.114.135939
- ↑ Bodon G, Chassefeyre R, Pernet-Gallay K, Martinelli N, Effantin G, Hulsik DL, Belly A, Goldberg Y, Chatellard-Causse C, Blot B, Schoehn G, Weissenhorn W, Sadoul R. Charged multivesicular body protein 2B (CHMP2B) of the endosomal sorting complex required for transport-III (ESCRT-III) polymerizes into helical structures deforming the plasma membrane. J Biol Chem. 2011 Nov 18;286(46):40276-86. doi: 10.1074/jbc.M111.283671. Epub, 2011 Sep 16. PMID:21926173 doi:http://dx.doi.org/10.1074/jbc.M111.283671
- ↑ Parkinson N, Ince PG, Smith MO, Highley R, Skibinski G, Andersen PM, Morrison KE, Pall HS, Hardiman O, Collinge J, Shaw PJ, Fisher EM. ALS phenotypes with mutations in CHMP2B (charged multivesicular body protein 2B). Neurology. 2006 Sep 26;67(6):1074-7. Epub 2006 Jun 28. PMID:16807408 doi:10.1212/01.wnl.0000231510.89311.8b
- ↑ Skalicky JJ, Arii J, Wenzel DM, Stubblefield WM, Katsuyama A, Uter NT, Bajorek M, Myszka DG, Sundquist WI. Interactions of the Human LIP5 Regulatory Protein with Endosomal Sorting Complexes Required for Transport. J Biol Chem. 2012 Oct 26. PMID:23105106 doi:http://dx.doi.org/10.1074/jbc.M112.417899
