Ubiquitin in the peroxisomal protein import pathway

被引:32
作者
Francisco, Tania [1 ,2 ]
Rodrigues, Tony A. [1 ,2 ]
Pinto, Manuel P. [1 ]
Carvalho, Andreia F. [1 ]
Azevedo, Jorge E. [1 ,2 ]
Grou, Claudia P. [1 ]
机构
[1] Univ Porto, Organelle Biogenesis & Funct Grp, IBMC, P-4150180 Oporto, Portugal
[2] Univ Porto, ICBAS, P-4050313 Oporto, Portugal
关键词
Ubiquitination; Peroxisome; PEX5; Thioester; Protein trafficking; SIGNAL TYPE-1 RECEPTOR; RING FINGER PROTEINS; TARGETING SIGNAL; SACCHAROMYCES-CEREVISIAE; CYCLING RECEPTOR; PTS1; RECEPTOR; CONSERVED CYSTEINE; MASS-SPECTROMETRY; RAT-LIVER; FUNCTIONAL-CHARACTERIZATION;
D O I
10.1016/j.biochi.2013.08.003
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
PEX5 is the shuttling receptor for newly synthesized peroxisomal matrix proteins. Alone, or with the help of an adaptor protein, this receptor binds peroxisomal matrix proteins in the cytosol and transports them to the peroxisomal membrane docking/translocation module (DTM). The interaction between cargo-loaded PEX5 and the DTM ultimately results in its insertion into the DTM with the concomitant translocation of the cargo protein across the organelle membrane. PEX5 is not consumed in this event; rather it is dislocated back into the cytosol so that it can promote additional rounds of protein transportation. Remarkably, the data collected in recent years indicate that dislocation is preceded by monoubiquitination of PEX5 at a conserved cysteine residue. This mandatory modification is not the only type of ubiquitination occurring at the DTM. Indeed, several findings suggest that defective receptors jamming the DTM are polyubiquitinated and targeted to the proteasome for degradation. (C) 2013 Elsevier Masson SAS. All rights reserved.
引用
收藏
页码:29 / 35
页数:7
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