期刊
FEBS LETTERS
卷 512, 期 1-3, 页码 19-24出版社
WILEY
DOI: 10.1016/S0014-5793(02)02286-X
关键词
p62; atypical protein kinase C; ubiquitin; scaffold; trafficking
资金
- NINDS NIH HHS [NS 33661] Funding Source: Medline
Several highly conserved p62 homologs have recently been isolated, e.g. the rat atypical protein kinase C-interacting protein (ZIP), the murine A170/signal transduction and adapter protein, and the human p62, a protein that binds the Src homology 2 domain of p56(lek). These proteins share striking similarity in amino acid sequence and structural motifs, thereby suggesting conserved functional properties. ZIP/p62 has been shown to play an important role as a scaffold leading to the activation of the transcription factor nuclear factor kappaB. In addition, a nuclear form of p62 has been characterized that can serve as a transcriptional co-activator. Moreover, p62 is capable of binding ubiquitin (Ub) non-covalently through its Ub-associated domain. In this review, we will focus on the structure and function of ZIP/p62. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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