2016
DOI: 10.1042/bst20160036
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Peroxisome protein import: a complex journey

Abstract: The import of proteins into peroxisomes possesses many unusual features such as the ability to import folded proteins, and a surprising diversity of targeting signals with differing affinities that can be recognized by the same receptor. As understanding of the structure and function of many components of the protein import machinery has grown, an increasingly complex network of factors affecting each step of the import pathway has emerged. Structural studies have revealed the presence of additional interactio… Show more

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Cited by 44 publications
(32 citation statements)
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“…The machinery that transports these proteins to the peroxisome matrix comprises many different components [4][5][6][7]. Most are exclusively dedicated to this taskthese belong to the so-called peroxin family [8].…”
Section: Introductionmentioning
confidence: 99%
“…The machinery that transports these proteins to the peroxisome matrix comprises many different components [4][5][6][7]. Most are exclusively dedicated to this taskthese belong to the so-called peroxin family [8].…”
Section: Introductionmentioning
confidence: 99%
“…One considerable difference of peroxisomal import to many other cellular protein import systems is that matrix proteins are imported post-translationally in a folded state, or even as protein complexes, across the peroxisomal membrane ( Walton et al. 1995 ; Baker et al. 2016 ).…”
Section: Introductionmentioning
confidence: 99%
“…It is well known that the sorting of proteins to peroxisomes mainly depends on either of two types of signal sequences, PTS1 and PTS2 (see Rucktäschel et al, 2011 ; Baker et al, 2016 ; Erdmann, 2016 for reviews and references within). The PTS1 as the most common one, is a tripeptide present at the C-termini of proteins and frequently ends with the sequence S-K-L or its variants with a consensus sequence S/A/C-K/R/H-L/M ( Gould et al, 1989 ; Lametschwandtner et al, 1998 ; Brocard and Hartig, 2006 ; Williams et al, 2012 ; see Dias et al, 2016 ; Meinecke et al, 2016 for reviews and references within).…”
Section: Discussionmentioning
confidence: 99%
“…The PTS1 as the most common one, is a tripeptide present at the C-termini of proteins and frequently ends with the sequence S-K-L or its variants with a consensus sequence S/A/C-K/R/H-L/M ( Gould et al, 1989 ; Lametschwandtner et al, 1998 ; Brocard and Hartig, 2006 ; Williams et al, 2012 ; see Dias et al, 2016 ; Meinecke et al, 2016 for reviews and references within). In contrast to PTS1, the PTS2 functions at internal locations, with a conserved non-apeptide in the N-terminal domain, such as R-L-X5-H-L, and R/K-L/V/I-X5-H/Q-L/A (X: any amino acid) ( Terlecky et al, 1995 ; Petriv et al, 2004 ; see Baker et al, 2016 ; Meinecke et al, 2016 for reviews and references within).…”
Section: Discussionmentioning
confidence: 99%