Human Fas-associated factor 1, interacting with ubiquitinated proteins and valosin-containing protein, is involved in the ubiquitin-proteasome pathway

Authors
Song, EJYim, SHKim, EKim, NSLee, KJ
Issue Date
2005-03
Publisher
AMER SOC MICROBIOLOGY
Citation
MOLECULAR AND CELLULAR BIOLOGY, v.25, no.6, pp.2511 - 2524
Abstract
Human Fas-associated factor 1 (hFAFI) is a novel protein having multiubiquitin-related domains. We investigated the cellular functions of hFAF1 and found that valosin-containing protein (VCP), the multiubiquitin chain-targeting factor in the degradation of the ubiquitin-proteasome pathway, is a binding partner of hFAF1. hFAF1 is associated with the ubiquitinated proteins via the newly identified N-terminal UBA domain and with VCP via the C-terminal UBX domain. The overexpression of hFAF1 and a truncated UBA domain inhibited the degradation of ubiquitinated proteins and increased cell death. These results suggest that hFAF1 binding to ubiquitinated protein and VCP is involved in the ubiquitin-proteasome pathway. We hypothesize that hFAF1 may serve as a scaffolding protein that regulates protein degradation in the ubiquitin-proteasome pathway.
Keywords
KAPPA-B-ALPHA; UBA DOMAIN; AAA-ATPASE; RAD23; DEGRADATION; PROTEOLYSIS; BINDING; P47; IDENTIFICATION; RECEPTORS; KAPPA-B-ALPHA; UBA DOMAIN; AAA-ATPASE; RAD23; DEGRADATION; PROTEOLYSIS; BINDING; P47; IDENTIFICATION; RECEPTORS
ISSN
0270-7306
URI
https://pubs.kist.re.kr/handle/201004/136724
DOI
10.1128/MCB.25.6.2511-2524.2005
Appears in Collections:
KIST Article > 2005
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