期刊
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
卷 1763, 期 12, 页码 1585-1591出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2006.09.007
关键词
Pex5p; Pex13p; SH3 domain; P-x-x-P motif; peroxisome; W-x-x-x-F/Y motif; protein import
The Src homology 3 (SH3) domain-containing peroxisomal membrane protein Pex 13p is an essential component of the import machinery for matrix proteins and forms a binding site for the peroxisomal targeting type I (PTS 1) receptor Pex5p. The interaction between these two proteins can be described as novel in several ways. In the yeasts Saccharomyces cerevisiae and Pichia pastoris, the SH3 domain itself is responsible for the interaction but not via the typical P-x-x-P motifs that are common to SH3 ligands as Pex5p lacks such a motif. Instead, a region of Pex5p containing a 1,V-x-x-x-F/Y motif is crucial for this binding. In mammals, again W-x-x-x-F/Y motifs appear to be important for the interaction but the SH3 domain seems not to be the site for Pex5p binding, this being located in the N-terminus of Pex 13p. Despite these differences in the details of the Pex 13p-Pex5p interaction, the association of the two proteins is a crucial step in Pex5p-mediated protein import into peroxisomes in both yeasts and mammals. (c) 2006 Elsevier B.V All rights reserved.
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