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Ossareh-Nazari B, et al.  (2010) The Rsp5 ubiquitin ligase and the AAA-ATPase Cdc48 control the ubiquitin-mediated degradation of the COPII component Sec23. Exp Cell Res 316(20):3351-7

Abstract: Ubp3/Bre5 complex is a substrate-specific deubiquitylating enzyme which mediates deubiquitylation of Sec23, a component of the COPII complex involved in the transport between endoplasmic reticulum and Golgi apparatus. Here we show that ubiquitylation of Sec23 is controlled by the Rsp5 ubiquitin ligase both in vivo and in vitro. We have recently identified Cdc48, a chaperone-like that plays a key role in the proteasomal escort pathway, as a partner of the Ubp3/Bre5 complex. We now found that cdc48 thermosensitive mutant cells not only accumulate ubiquitylated form of Sec23 but also display a stabilization of this protein at the restrictive temperature. This indicates that Cdc48 controls the proteasome-mediated degradation of Sec23. Our data favor the idea that Cdc48 plays a key role in deciphering fates of ubiquitylated Sec23 to degradation or deubiquitylation/stabilization via its cofactors.CI - Copyright (c) 2010 Elsevier Inc. All rights reserved.

Status: Published Type: Journal Article | Research Support, Non-U.S. Gov't PubMed ID: 20846524

Topics addressed in this paper

Number of different genes curated to this paper: 16

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Topics Genes linked to topics (#1 - 10 )
BRE5 CDC48 DOA1 NPL4 RSP5 SEC23 SHP1 UBA1 UBC4 UBP3
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Substrates/Ligands/Cofactors blue ball blue ball blue ball blue ball blue ball blue ball

Topics Genes linked to topics (#11 - 16 )
UBX2 UBX3 UBX4 UBX5 UBX6 UBX7
Mutants/Phenotypes blue ball blue ball blue ball blue ball blue ball blue ball
Primary Literature blue ball blue ball blue ball blue ball blue ball blue ball

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