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Vacuolar protein sorting-associated protein: Difference between revisions

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== Function ==
== Function ==


'''Vacuolar protein sorting-associated protein''' (Vps) are part of '''E'''ndosomal '''S'''orting '''C'''omplex '''R'''equired for '''T'''ransport ('''ESCRT''') 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>.
'''Vacuolar protein sorting-associated protein''' (Vps) are part of '''E'''ndosomal '''S'''orting '''C'''omplex '''R'''equired for '''T'''ransport ('''ESCRT''') 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>.  The '''retromer''' comprises 2 functional subcomplexes: the cargo-selective one which contains Vps35, Vps29 and Vps26 and the sorting nexin subcomplex which tubulate the endosomal membrane<ref>PMID:19531583</ref>. The Vps proteins are found in yeast.  The human homologs are called also '''chromatin-modifying protein''' or [[Charged multivesicular body protein]] ('''CHMP''')<ref>PMID:16730941</ref>.
*'''Vps4''', '''Vps4A''', ''Vps4B'' complex catalyzes the disassembly of the ESCRT-III filament in an ATP-driven reaction.  Vps4 proteins are required for centrosome and spindle maintenance<ref>PMID:20616062</ref>.<br />
*'''Vps4''', '''Vps4A''', ''Vps4B'' complex catalyzes the disassembly of the ESCRT-III filament in an ATP-driven reaction.  Vps4 proteins are required for centrosome and spindle maintenance<ref>PMID:20616062</ref>.<br />
*'''Vps9A''' activates Rab5 to GTP-bound form<ref>PMID:18055610</ref>.<br />
*'''Vps9A''' activates Rab5 to GTP-bound form<ref>PMID:18055610</ref>.<br />
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== Disease ==
== Disease ==


Mutations in Vps53 cause progressive cerebello-cerebral atrophy type 2<ref>PMID:24577744</ref>.  Mutations in Vps54 in mice cause motor neuron disease<ref>PMID:16244655</ref>.
Mutations in '''Vps53''' cause progressive cerebello-cerebral atrophy type 2<ref>PMID:24577744</ref>.  Mutations in '''Vps54''' in mice cause motor neuron disease<ref>PMID:16244655</ref>. Dysfunction of the '''retromer''' is implicated in neurodegenerative disease like Alzheimer disease, Parkinson's disease and Frontotemporal lobar degeneration<ref>PMID:29755290</ref>.


== Relevance ==
== Relevance ==
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</StructureSection>
</StructureSection>


==3D structures of vacuolar protein sorting-associated protein==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*Vps4 domains: MIT 1-82; AAA ATPase 124-437
**[[5xmi]] – yVps4 + ATP – yeast - Cryo EM<br />
**[[2rko]] – yVps4 AAA ATPase domain<br />
**[[3eie]] – yVps4 AAA ATPase domain (mutant)<br />
**[[3eih]] – yVps4 AAA ATPase domain (mutant) + ATPγS<br />
**[[2qp9]] – yVps4 83-437<br />
**[[2qpa]] – yVps4 (mutant) 83-437 + ADP<br />
**[[2v6x]] – yVps4 MIT domain + yVps2 C-terminal<br />
**[[4niq]], [[5fvk]] – yVps4 MIT domain + yVfa1 MIM2 domain<br />
**[[5fvl]] – yVps4 MIT domain + yVPS20 <br />
**[[3mhv]] – yVps4 + yVps Vta1 <br />
**[[6ap1]] – yVps4 + yVps Vta1 + peptide<br />
**[[6oo2]], [[6ndy]] – yVps4 + yVps Vta1 + peptide - Cryo EM<br />
**[[5uie]] – yVps4 + yVps2 + yVps Vta1 – Cryo EM<br />
**[[5xmk]] – yVps4 (mutant) + yVps Vta1 + ATP – Cryo EM<br />
**[[6bmf]] – yVps4 AAA ATPase domain + yVps2P – Cryo EM<br />
*Vps4A
**[[1yxr]] – hVps4A MIT domain – human - NMR<br />
**[[2jq9]] – hVps4A MIT domain + CHMP1A peptide - NMR<br />
**[[2k3w]] – yVps4A MIT domain + CHMP6 peptide - NMR<br />
*Vps4B or Skd1
**[[2jqh]], [[2cpt]], [[1wr0]] – hVps4B MIT domain - NMR<br />
**[[1xwi]] – hVps4B C-terminal<br />
**[[4u7y]] – hVps4B MIT domain + IST1 peptide<br />
**[[2jqk]] – hVps4B MIT domain + CHMP2B<br />
**[[2zam]] – mVps4B - mouse<br />
**[[2zao]] – mVps4B + ADP<br />
**[[2zan]] – mVps4B + ATP<br />
*Vps9
**[[1mn3]] – yVps9 CUE domain 398-451<br />
**[[1p3q]] – yVps9 CUE domain + ubiquitin<br />
*Vps9A
**[[4g01]] – Vps9A + RABF2B – ''Arabidopsis thaliana''<br />
*Vps13
**[[6cbc]] – CtVps13 N-terminal (mutant) – ''Chaetomium thermophilum'' <br />
*Vps15 or serine/threonine protein kinase Vps15
**[[3gre]] – yVps15 WD repeat domain <br />
*Vps23
**[[2f6m]] – yVps23 C-terminal (mutant) + yVps28 N-terminal<br />
**[[3r42]] – yVps23 N-terminal (mutant) + yVps27 peptide <br />
**[[2caz]] – yVps23 + yVps28 N-terminal + SRN2 <br />
**[[2f66]] – yVps23 C-terminal + yVps28 N-terminal + SRN2<br />
**[[2p22]] – yVps23 + yVps28 N-terminal + SRN2 + peptide  <br />
**[[1uzx]] – yVps23 UEV domain 1-161 + ubiquitin <br />
*Vps25
**[[3htu]] – hVps23 C-terminal WH2 domain + hVps20 first helix <br />
*Vps 26A
**[[6md5]] – Vps26A – zebrafish<br />
**[[4p2a]] – mVps26A + sorting nexin-3 <br />
*Vps26B
**[[3lh8]], [[2r51]] – mVps26B <br />
**[[3lh9]], [[3lha]] – mVps26B (mutant)<br />
*Vps26-like
**[[6h7w]] – CtVps26L + Vsp29 + Vsp35 - Cryo EM<br />
*Vps27
**[[2pjw]] – yVps27 C-terminal + protein<br />
**[[6njg]] – yVps27 + polyubiquitin<br />
*Vps28
**[[2g3q]], [[2j9v]] – yVps28 C-terminal <br />
**[[2j9u]] – yVps28 + yVps36 <br />
*Vps29
**[[5wyh]] – hVps29 + interaptin<br />
**[[5osh]], [[5osi]] – hVps29 + hVps35 + interaptin<br />
**[[5gtu]] – hVps29 + TBC1D5<br />
**[[3psn]], [[3pso]] – mVps29 <br />
**[[6vab]] – mVps29 + mVps35 - Cryo EM <br />
**[[2r17]] – yVps29 + yVps35 <br />
**[[5xce]], [[5xch]] – EhVps29 – ''Entamoeba histolytica'' <br />
**[[5xcj]], [[5xck]] – EhVps29 (mutant)<br />
**[[5w8m]] – CtVps29  <br />
**[[6h7w]] – CtVps29 + CtVps35 + CtVps26-like + CtVPS - Cryo EM<br />
*Vps30
**[[3vp7]] – hVps30 C-terminal <br />
*Vps33
**[[5bv1]] – CtVps33 + CtVps16 <br />
**[[5bv0]] – CtVps33 + CtVps16 <br />
*Vps33A
**[[4bx8]] – hVps33A <br />
**[[4bx9]] – hVps33A + hVps16 C-terminal + SNARE domain<br />
*Vps34
**[[5dfz]] – yVps34 + yVps38 + yVps15 + yVps30 + nanobody<br />
*Vps35
**[[5f0k]] – hVps35 N-terminal <br />
**[[5f0j]] – hVps35 + hVps26A + sorting nexin-3 <br />
**[[5f0l]], [[5f0m]], [[5f0p]] – hVps35 + hVps26A + sorting nexin-3 + DMT-1<br />
**[[6vac]] – mVps35 + mVps26A + mVps29 - Cryo EM<br />
*Vps36
**[[5kc2]] – yVps36 + yVps15 <br />
**[[2hth]] – hVps36 GLUE domain 1-138 + ubiquitin <br />
**[[2zme]], [[3cuq]] – hVps36 + hVps25 + SNF8 <br />
*Vps46
**[[3ggz]] – yVps46 MIM motif 176-204 + IST1 <br />
*Vps53
**[[3ns4]] – yVps53 C-terminal <br />
*Vps54
**[[3n1b]] – yVps54 C-terminal <br />
**[[3n1e]] – mVps54 C-terminal <br />
*Vps60
**[[2luh]] – yVps60 + yVps Vta1 - NMR <br />
*Vps72
**[[6gej]], [[6gen]] – yVps72 in nucleosome – Cryo EM<br />
*Vps72 homolog
**[[5chl]] – Vps72 + histone H2A.Z – ''Drosophila melanogaster'' <br />
**[[5fug]] – hVps72 N-terminal + histone H2A.Z <br />
*Vps74
**[[2zih]], [[2zii]] – yVps74<br />
**[[4tu3]] – yVps74 + SAC1<br />
*Vps75
**[[3c9b]], [[3c9d]], [[5agc]] – yVps75 <br />
**[[3dm7]] – yVps75 (mutant)<br />
**[[2zd7]] – yVps75 + peptide  <br />
**[[3q68]], [[3q66]] – yVps75 + histone acetyltransferase  <br />
**[[3q33]] – yVps75 + histone acetyltransferase + histone H3 peptide <br />
**[[6o22]] – yVps75 + histone acetyltransferase + histone H3 peptide + histone H4 peptide + ASF1 - NMR<br />
**[[3q35]] – yVps75 + histone acetyltransferase + acetyl CoA<br />
**[[5yps]] – Vps75 (mutant) – ''Pneumocystis carinii''<br />
*Vps Vta1 or Lip5
**[[2lxl]] – hVps Vta1 <br />
**[[4txp]] – hVps Vta1 N-terminal <br />
**[[2rkk]] – yVps Vta1 N-terminal <br />
**[[2rkl]] – yVps Vta1 C-terminal <br />
**[[5h7p]] – yVps Vta1 N-terminal + yVps46 D1-D2 domain - NMR<br />
**[[4u7e]] – hVps Vta1 N-terminal + IST1<br />
**[[2lxm]] – hVps Vta1 N-terminal + CHMP5<br />
**[[4txq]] – hVps Vta1 N-terminal + CHMP1B<br />
**[[4txr]] – hVps Vta1 N-terminal + CHMP1B + CHMP5<br />
}}
== References ==
== References ==
<references/>
<references/>


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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky
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