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Complex: VPS4 complex

Macromolecular complex annotations are imported from the Complex Portal. These annotations have been derived from physical molecular interaction evidence extracted from the literature and cross-referenced in the entry, or by curator inference from information on homologs in closely related species or by inference from scientific background.

Curated by
IntAct
ComplexAc
CPX-334
Systematic Name
VPS4 oligomer
SGD ID
SGD:S000217679
Aliases
ESCRT-IV complex ; Endosomal sorting complex required for transport-IV complex ; Vacuolar protein sorting-associated complex
Description
An AAA-ATPase that is probably the main energy-providing system for the membrane deformation and abscission function of the ESCRT machinery consisting of ESCRT-0 (CPX-1622), -I (CPX-940), -II (CPX-1623), -III (CPX-1624) and -IV (this complex) . Required for the dissociation and recycling of ESCRT-III complex subunits from vesicle and plasma membranes as well as the midbody during the final stages of cytokinesis where it causes constriction of the ESCRT-III polymer and fission of the associated membrane neck. Multiple disassembly reactions are performed until ESCRT-III dissociation has been completed. VPS4 ATPase activity is regulated by a) ESCRT-III interactions with VPS4 which enhance ATP hydrolysis by relieving autoinhibition of the AAA domain and b) binding of the VTA1 homodimers (Q06263) which both promotes VPS4 oligomerization and enhances ATP hydrolysis. Binding of ESCRT-III subunits DID2 (P69771) or VPS60 (Q03390) to the amino-terminal of VTA1 relieves autoinhibition within VTA1 to further enhance stimulation of VPS4 ATP hydrolysis. Binding of IST1 (P53843) to VPS4 negatively regulates VPS4 activity by blocking binding to the ESCRT machinery.

Complex Diagram

This diagram displays the protein subunits (blue) of the complex and how they interact with each other. Interactions with other relevant participants such as small molecules (purple), sub-complexes (yellow), and other subunits (red) are also shown. If a participant appears in the diagram with no lines connected to it, then its specific interactions with other participants are currently unknown.

PDB Structure

When available from the Protein Data Bank (PDB), the physical structure of the macromolecular complex is displayed. Click on the image or link for further information about the physical structure.

2RKO 2RKO

Subunits

This table lists all participants of the complex (proteins, small molecules, nucleic acids, etc.) and their respective stoichiometry. A brief description is also provided for each participant in the table.

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Subunit Description Stoichiometry

Gene Ontology

Gene Ontology (GO) terms that describe the function of a complex, the biological process in which it participates, or its cellular location. Click on a term for its definition and other objects annotated to that term.

Shared Annotations

This diagram displays Gene Ontology terms (green) and subunits (blue) that are shared between the given macromolecular complex (black) and other yeast complexes (yellow). The shared GO terms or subunits can be visualized separately using the radio button at the bottom of the graph. Note: No diagram is shown ("No shared annotations") if there are less than 2 shared annotations (either GO terms or subunits of other complexes) between this complex and any other complexes.

References

List of references used specifically to curate the information on this page.

External Identifiers

EMDB: 1481 | EMDB: 5040 | IntEnz: 3.6.4.6

Resources

IntAct | ModelArchive | PDB:2RKO