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Title 

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

Authors 

E J SongS H YimE KimNam-Soon KimK J Lee

Publisher 

American Society for Microbiology

Issue Date 

2005

Citation 

Molecular and Cellular Biology, vol. 25, no. 6, pp. 2511-2524

Keywords 

fas antigenproteasomescaffold proteinubiquitinhumanhuman cellprotein bindingprotein degradationprotein domainprotein expression

Abstract 

Human Fas-associated factor 1 (hFAF1) 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.

ISSN 

0270-7306

Link 

http://dx.doi.org/10.1128/MCB.25.6.2511-2524.2005

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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