Charged multivesicular body protein

Function Charged multivesicular body protein (CHMP)s are part of Endosomal Sorting Complex Required for Transport (ESCRT) together with the Vacuolar protein sorting-associated proteins 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. CHMPs are part of the ESCRT-III complex. CHMP1A and CHMP2B are required for bodies containing plastid material during autophagy into the cytoplasm . CHMP2B polimerization scaffolds membranes as part of outward membrane deformation. 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.

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3D structures of charged multivesicular body protein3D structures of charged multivesicular body protein

Updated on 18-December-2018

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• CHMP1B
  • 4txq – hCHMP1B MIM domain + hVps Vta1 N-terminal - human
    
  • 4txr – hCHMP1B MIM domain + hVps Vta1 N-terminal + CHMP5
    
  • 6e8g, 3jc1 – hCHMP1B + IST1 + DNA – Cryo EM
    
  • 2xze – hCHMP1B C-terminal + STAM-binding protein
    
• CHMP3
  • 2gd5, 3frt, 3frv – hCHMP3
    
• CHMP4A
  • 5mk1, 5mk2 – hCHMP4A + tyrosine phosphatase
    
• CHMP4B
  • 4abm – hCHMP4B hairpin
    
  • 3um3 – hCHMP4B C-terminal + BROX
    
• CHMP4C
  • 5mk3 – hCHMP4C + tyrosine phosphatase
    
• CHMP5
  • 2lxm – hCHMP5 residues 139-195 + hVps Vta1 N-terminal
    
  • 3uly, 3um0, 3um1, 3um2 – hCHMP5 C-terminal + BROX