Song, EJ Yim, SH Kim, E Kim, NS Lee, KJ 2024-01-21T05:32:47Z 2024-01-21T05:32:47Z 2021-09-01 2005-03 0270-7306 https://pubs.kist.re.kr/handle/201004/136724 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. English AMER SOC MICROBIOLOGY KAPPA-B-ALPHA UBA DOMAIN AAA-ATPASE RAD23 DEGRADATION PROTEOLYSIS BINDING P47 IDENTIFICATION RECEPTORS Human Fas-associated factor 1, interacting with ubiquitinated proteins and valosin-containing protein, is involved in the ubiquitin-proteasome pathway Article 10.1128/MCB.25.6.2511-2524.2005 1 MOLECULAR AND CELLULAR BIOLOGY, v.25, no.6, pp.2511 - 2524 MOLECULAR AND CELLULAR BIOLOGY 25 6 2511 2524 scie scopus 000227475300037 2-s2.0-14844340788 Biochemistry & Molecular Biology Cell Biology Biochemistry & Molecular Biology Cell Biology Article KAPPA-B-ALPHA UBA DOMAIN AAA-ATPASE RAD23 DEGRADATION PROTEOLYSIS BINDING P47 IDENTIFICATION RECEPTORS