Valosin-containing protein

Transitional endoplasmic reticulum ATPase (TER ATPase) also known as valosin-containing protein (VCP) is an is_associated_with::enzyme that in humans is encoded by the VCP is_associated_with::gene.

Function
Valosin-containing protein (VCP) is a type II member of AAA+-ATPase family. It functions as a ubiquitin segregase that remodels multimeric protein complexes by extracting polyubiquitinated proteins for recycling or degradation by the proteasome. VCP subserves a broad array of cellular functions including mitochondrial quality control, autophagy, vesicle transport and fusion, 26S is_associated_with::proteasome function, and assembly of is_associated_with::peroxisomes. VCP, as a structural protein, is associated with is_associated_with::clathrin, and heat-shock protein is_associated_with::Hsc70, to form a complex. VCP has been implicated in a number of cellular events that are regulated during mitosis, including homotypic membrane fusion, is_associated_with::spindle pole body function, and is_associated_with::ubiquitin-dependent protein degradation.

Interactions
Valosin-containing protein has been shown to interact with is_associated_with::AMFR, SELS,  is_associated_with::BRCA1, is_associated_with::NSFL1C, is_associated_with::IκBα and is_associated_with::Ataxin 3.

Clinical significance
Mutations in VCP are causative of a pleiotropic degenerative disorder called is_associated_with::multisystem proteinopathy or "MSP" that can affect muscle, bone and/or the central nervous system. MSP can manifest clinically as classical amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), inclusion body myopathy (IBM), Paget's disease of bone (PDB), or as a combination of these disorders.