Charged multivesicular body protein: Difference between revisions

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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
<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 ==
== 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 '''CHMP2B''' are required for bodies containing plastid material during autophagy into the cytoplasm <ref>PMID:25649438</ref>.<br />
*'''CHMP1A''' and '''CHMP1B''' are required for bodies containing plastid material during autophagy into the cytoplasm <ref>PMID:25649438</ref>.<br />
*'''CHMP2B''' polimerization scaffolds membranes as part of outward membrane deformation<ref>PMID:21926173</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.
*'''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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Mutations in CHMP2B are implicated in ALS<ref>PMID:16807408</ref>.
Mutations in CHMP2B are implicated in ALS<ref>PMID:16807408</ref>.
== Relevance ==


== Structural highlights ==
== 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>.
</StructureSection>


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


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*CHMP1B
 
**[[4txq]] – hCHMP1B MIM domain + hVps Vta1 N-terminal - human<br />
**[[4txr]] – hCHMP1B MIM domain + hVps Vta1 N-terminal + CHMP5<br />
**[[6e8g]], [[3jc1]] – hCHMP1B + IST1 + DNA – Cryo EM<br />
**[[2xze]] – hCHMP1B C-terminal + STAM-binding protein<br />
 
*CHMP3
 
**[[2gd5]], [[3frt]], [[3frv]] – hCHMP3<br />
 
*CHMP4A
 
**[[5mk1]], [[5mk2]] – hCHMP4A + tyrosine phosphatase<br />
 
*CHMP4B
 
**[[4abm]] – hCHMP4B hairpin<br />
**[[3um3]] – hCHMP4B C-terminal + BROX<br />
 
*CHMP4C
 
**[[5mk3]] – hCHMP4C + tyrosine phosphatase<br />
 
*CHMP5
 
**[[2lxm]] – hCHMP5 residues 139-195 + hVps Vta1 N-terminal <br />
**[[3uly]], [[3um0]], [[3um1]], [[3um2]] – hCHMP5 C-terminal + BROX<br />


}}
== References ==
== References ==
<references/>
<references/>


[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 10:32, 3 June 2024


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[1]. CHMPs are part of the ESCRT-III complex.

  • CHMP1A and CHMP1B are required for bodies containing plastid material during autophagy into the cytoplasm [2].
  • CHMP2B polymerization scaffolds membranes as part of outward membrane deformation[3].
  • 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[4].

Structural highlights

The ampiphatic CHMP5 creates a hydrophobic binding collar that includes which make . A 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[5].

3D structures of charged multivesicular body protein

Charged multivesicular body protein 3D structures


Human CHMP5 residues 139-195 (green) complex with vacuolar protein sorting-associated protein Vta1 homolog (cyan) (PDB code 2lxm)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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

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