| Literature DB >> 25447673 |
Changcheng Song1, Qing Wang2, Changzheng Song3, Stephen J Lockett4, Nancy H Colburn5, Chou-Chi H Li6, Ji Ming Wang7, Thomas J Rogers8.
Abstract
Valosin-containing protein (VCP or p97), a member of the AAA family (ATPases associated with diverse cellular activities), plays a key role in many important cellular activities. A genetic deficiency of VCP can cause inclusion body myopathy associated with Paget's disease of bone and frontotemporal dementia (IBMPFD). Previous studies showed that the VCP N domain is essential for the regulation of nuclear entry of VCP. Here we report that IBMPFD mutations, which are mainly located in the N domain, suppress the nuclear entry of VCP. Moreover, the peptide sequence G780AGPSQ in the C-terminal region regulates the retention of VCP in the nucleus. A mutant lacking this sequence can increase the nuclear distribution of IBMPFD VCP, suggesting that this sequence is a potential molecular target for correcting the deficient nucleocytoplasmic shuttling of IBMPFD VCP proteins.Entities:
Keywords: Inclusion body myopathy associated with Paget's disease of bone and frontotemporal dementia (IBMPFD); Nuclear export signal; Nucleocytoplasmic shuttling; Valosin containing protein
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Year: 2014 PMID： 25447673 PMCID： PMC4254625 DOI： 10.1016/j.bbamcr.2014.10.019
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002