Pex14p, more than just a docking protein

被引:60
作者
Azevedo, Jorge E.
Schliebs, Wolfgang
机构
[1] Univ Porto, Inst Biol Mol & Celular, P-4100 Oporto, Portugal
[2] Univ Porto, Inst Ciencias Biomed Abel Salazar, P-4100 Oporto, Portugal
[3] Ruhr Univ Bochum, Inst Physiol Chem, Abt Systembiochem, D-44780 Bochum, Germany
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2006年 / 1763卷 / 12期
关键词
peroxisome; protein import; PTS1-receptor; Pex5p; Pex14p; importomer; PEROXISOMAL MEMBRANE-PROTEIN; TARGETING SIGNAL-RECEPTOR; N-TERMINAL HALF; SACCHAROMYCES-CEREVISIAE; PTS1; RECEPTOR; IMPORT MACHINERY; CYCLING RECEPTOR; BINDING-SITES; SH3; DOMAIN; PICHIA-PASTORIS;
D O I
10.1016/j.bbamcr.2006.09.002
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
After binding newly synthesized peroxisomal matrix proteins in the cytosol, the second task of Pex5p, the peroxisomal cycling receptor, is to carry these proteins to the peroxisomal membrane. Defining the nature of the events that occur at this membrane system and which ultimately result in the translocation of the cargo proteins into the matrix of the organelle and in the recycling of Pex5p back to the cytosol, is one of the major goals of the research in this field. Presently, it is generally accepted that all these steps are promoted by a large protein complex embedded in the peroxisomal membrane. This docking/translocation machinery or importomer, as it is often called, comprises many different peroxins of which one of the best characterized is Pex 14p. Here, we review data regarding this membrane peroxin with emphasis on the interactions that it establishes with Pex5p. The available evidence suggests that the key to understand how folded proteins are capable of passing an apparently impermeable membrane may largely reside in this pair of peroxins. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:1574 / 1584
页数:11
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