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Review
. 2013:2013:183421.
doi: 10.1155/2013/183421. Epub 2013 Sep 15.

Cdc48: a swiss army knife of cell biology

Guem Hee Baek  1 , Haili Cheng, Vitnary Choe, Xin Bao, Jia Shao, Shiwen Luo, Hai Rao
Affiliations
Review

Cdc48: a swiss army knife of cell biology

Guem Hee Baek et al. J Amino Acids. 2013.

Abstract

Cdc48 (also called VCP and p97) is an abundant protein that plays essential regulatory functions in a broad array of cellular processes. Working with various cofactors, Cdc48 utilizes its ATPase activity to promote the assembly and disassembly of protein complexes. Here, we review key biological functions and regulation of Cdc48 in ubiquitin-related events. Given the broad employment of Cdc48 in cell biology and its intimate ties to human diseases (e.g., amyotrophic lateral sclerosis), studies of Cdc48 will bring significant insights into the mechanism and function of ubiquitin in health and diseases.

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Figures

Figure 1
Figure 1
Number of papers on Cdc48 published since 1982. Key words “Cdc48, VCP, and p97” were used to search PUBMED for papers on Cdc48 from 1982 to 2012.
Figure 2
Figure 2
Structural and functional organization of Cdc48. (a) Cdc48 consists of the conserved N-terminal domain (N), two conserved AAA ATPase domains (D1 and D2), and the C-terminal domain (C). The numbers refer to the amino acid positions within the protein in yeast and human Cdc48, respectively. Cofactors associated with the N and C domains are listed. Yeast proteins, nearly all of which have human homologues, are highlighted in italics. (b) The active Cdc48 is a ring-shaped hexamer. (c) Cdc48 and its cofactors assemble in a Swiss army knife manner.
See this image and copyright information in PMC

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