View source for Charged multivesicular body protein

<StructureSection load='2lxm' size='340' side='right' caption='Human CHMP5 residues 139-195 (green) complex with vacuolar protein sorting-associated protein Vta1 homolog (cyan) (PDB code [[2lxm]])' scene='80/803956/Cv/1'>

== 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.  

*'''CHMP1A''' and '''CHMP1B''' are required for bodies containing plastid material during autophagy into the cytoplasm <ref>PMID:25649438</ref>.<br />
*'''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.
*'''CHMP5''' has possibly a regulatory role on apoptosis-associated genes.

== Disease ==

Mutations in CHMP2B are implicated in ALS<ref>PMID:16807408</ref>.

== Structural highlights ==

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>.

==3D structures of charged multivesicular body protein==
[[Charged multivesicular body protein 3D structures]]

</StructureSection>

== References ==
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