Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein

Pleasure, Irene T.; Black, Mark M.; Keen, James H.

doi:10.1038/365459a0

Cited by 123 publications

(79 citation statements)

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“…Interestingly, VCP also forms stable cytosolic complexes with clathrin and Hsp70 (Pleasure et al, 1993). The demonstration that VCP binds to clathrin, its homology to proteins involved in membrane transport, and its similarity to GroEL chaperonins suggest that VCP functions in a subset of clathrinmediated membrane transfer reactions through ATPdependent modulation of protein-protein interactions (Pleasure et al, 1993). Here, we show that p532 also forms stable complexes with clathrin and Hsp70.…”

Section: Discussionmentioning

confidence: 72%

“…The valosin-containing protein (VCP) was identi®ed as an early substrate for tyrosine phosphorylation following T-cell receptor activation (Egerton et al, 1992). Interestingly, VCP also forms stable cytosolic complexes with clathrin and Hsp70 (Pleasure et al, 1993). The demonstration that VCP binds to clathrin, its homology to proteins involved in membrane transport, and its similarity to GroEL chaperonins suggest that VCP functions in a subset of clathrinmediated membrane transfer reactions through ATPdependent modulation of protein-protein interactions (Pleasure et al, 1993).…”

Section: Discussionmentioning

confidence: 99%

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A giant protein that stimulates guanine nucleotide exchange on ARF1 and Rab proteins forms a cytosolic ternary complex with clathrin and Hsp70

Rosa

Barbacid

1997

Oncogene

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We have recently identi®ed an unusually large human protein that stimulates guanine nucleotide exchange on ARF1 and Rab proteins (EMBO J 15: 4262 ± 4273, 1996). This protein, designated p532 based on its predicted molecular weight (EMBO J 15: 5738, 1996), contains multiple structural domains including two regions of seven internal repeats highly related to the cell cycle regulator RCC1, a guanine nucleotide exchange factor for the small GTP-binding protein Ran, seven b-repeat domains characteristic of the b subunit of heterotrimeric G proteins, three putative SH3 binding sites, a putative leucine-zipper and a carboxyterminal HECT domain characteristic of E3 ubiquitinprotein ligases. Some of these domains are known to be involved in protein-protein interactions, suggesting the existence of p532-interacting proteins. To identify some of these proteins, we used the carboxy-terminal RCC1-like domain (RLD) of p532 in the yeast two-hybrid system. We report here the isolation of a clone that encodes the last 654 amino acid residues of the clathrin heavy chain. This interaction involves amino acid residues 1315 ± 1557 of the clathrin heavy chain and the carboxy, but not the amino-terminal RLD of p532. p532 has been located in the cytosolic fraction as well as in the Golgi apparatus. The interaction between p532 and clathrin only occurs in the cytosol and is mediated by the formation of an ATP-dependent ternary complex with the heat shock protein, Hsp70. These observations suggest that p532 is involved in membrane transport processes.

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Section: Discussionmentioning

confidence: 72%

Section: Discussionmentioning

confidence: 99%

A giant protein that stimulates guanine nucleotide exchange on ARF1 and Rab proteins forms a cytosolic ternary complex with clathrin and Hsp70

Rosa

Barbacid

1997

Oncogene

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“…This process further requires the activity of another member of this group of AAA proteins, VCP/p97 (the homologue of yeast Cdc48), at a later stage of the process (Acharya et al 1995;Rabouille et al 1995). VCP/p97 also interacts with the vesicle-coating protein clathrin (Pleasure et al 1993) and in human T-cells is tyrosine-phosphorylated in response to proliferation signals (Schulte et al 1994). The Pas genes affect the import of protein into peroxisomes, and appear to be involved in membrane addition to the peroxisome.…”

Section: The Membrane Fusion Proteinsmentioning

confidence: 99%

The Evolution of the Conserved ATPase Domain (CAD): Reconstructing the History of an Ancient Protein Module

Swaffield

Purugganan

1997

J Mol Evol

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Abstract. The AAA proteins (ATPases Associated with a variety of cellular Activities) are found in eubacterial, archaebacterial, and eukaryotic species and participate in a large number of cellular processes, including protein degradation, vesicle fusion, cell cycle control, and cellular secretory processes. The AAA proteins are characterized by the presence of a 230 to 250-amino acid ATPase domain referred to as the Conserved ATPase Domain or CAD. Phylogenetic analysis of 133 CAD sequences from 38 species reveal that AAA CADs are organized into discrete groups that are related not only in structure but in cellular function. Evolutionary analyses also indicate that the CAD was present in the last common ancestor of eubacteria, archaebacteria, and eukaryotes. The eubacterial CADs are found in metalloproteases, while CAD-containing proteins in the archaebacterial and eukaryotic lineages appear to have diversified by a series of gene duplication events that lead to the establishment of different functional AAA proteins, including proteasomal regulatory, NSF/Sec, and Pas proteins. The phylogeny of the CADs provides the basis for establishing the patterns of evolutionary change that characterize the AAA proteins.

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“…Thus, adaptor selection appears to dictate the enrollment of p97 into different cellular pathways [4,15]. In this regard, it is interesting to note that the endocytic adaptor protein clathrin was the first identified p97-interacting protein [16]. Nonetheless, whether p97 plays a role in endocytic regulation has remained unclear.…”

Section: Introductionmentioning

confidence: 99%

The p97 ATPase associates with EEA1 to regulate the size of early endosomes

Ramanathan

2011

Cell Res

100

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The AAA (ATPase-associated with various cellular activities) ATPase p97 acts on diverse substrate proteins to partake in various cellular processes such as membrane fusion and endoplasmic reticulum-associated degradation (ERAD). In membrane fusion, p97 is thought to function in analogy to the related ATPase NSF (N-ethylmaleimidesensitive fusion protein), which promotes membrane fusion by disassembling a SNARE complex. In ERAD, p97 dislocates misfolded proteins from the ER membrane to facilitate their turnover by the proteasome. Here, we identify a novel function of p97 in endocytic trafficking by establishing the early endosomal autoantigen 1 (EEA1) as a new p97 substrate. We demonstrate that a fraction of p97 is localized to the early endosome membrane, where it binds EEA1 via the N-terminal C2H2 zinc finger domain. Inhibition of p97 either by siRNA or a pharmacological inhibitor results in clustering and enlargement of early endosomes, which is associated with an altered trafficking pattern for an endocytic cargo. Mechanistically, we show that p97 inhibition causes increased EEA1 self-association at the endosome membrane. We propose that p97 may regulate the size of early endosomes by governing the oligomeric state of EEA1.

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Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein

Cited by 123 publications

References 0 publications

A giant protein that stimulates guanine nucleotide exchange on ARF1 and Rab proteins forms a cytosolic ternary complex with clathrin and Hsp70

A giant protein that stimulates guanine nucleotide exchange on ARF1 and Rab proteins forms a cytosolic ternary complex with clathrin and Hsp70

The Evolution of the Conserved ATPase Domain (CAD): Reconstructing the History of an Ancient Protein Module

The p97 ATPase associates with EEA1 to regulate the size of early endosomes

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