نتایج جستجو برای: peroxin

تعداد نتایج: 177  

Journal: :The Journal of Cell Biology 1998
P. Edward Purdue Xudong Yang Paul B. Lazarow

We have identified ScPex18p and ScPex21p, two novel S. cerevisiae peroxins required for protein targeting via the PTS2 branch of peroxisomal biogenesis. Targeting by this pathway is known to involve the interaction of oligopeptide PTS2 signals with Pex7p, the PTS2 receptor. Pex7p function is conserved between yeasts and humans, with defects in the human protein causing rhizomelic chondrodysplas...

Journal: :The Journal of biological chemistry 2004
João Costa-Rodrigues Andreia F Carvalho Alexandra M Gouveia Marc Fransen Clara Sá-Miranda Jorge E Azevedo

Most newly synthesized peroxisomal matrix proteins are transported to the organelle by Pex5p, a remarkable multidomain protein involved in an intricate network of transient protein-protein interactions. Presently, our knowledge regarding the structure/function of amino acid residues 118 to the very last residue of mammalian Pex5p is quite vast. Indeed, the cargo-protein receptor domain as well ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2011
Shusuke Yonekawa Akiko Furuno Takashi Baba Yukio Fujiki Yuta Ogasawara Akitsugu Yamamoto Mitsuo Tagaya Katsuko Tani

Sec16 plays a key role in the formation of coat protein II vesicles, which mediate protein transport from the endoplasmic reticulum (ER) to the Golgi apparatus. Mammals have two Sec16 isoforms: Sec16A, which is a longer primary ortholog of yeast Sec16, and Sec16B, which is a shorter distant ortholog. Previous studies have shown that Sec16B, as well as Sec16A, defines ER exit sites, where coat p...

Journal: :The Journal of Cell Biology 2002
Vladimir I. Titorenko Jean-Marc Nicaud Huijie Wang Honey Chan Richard A. Rachubinski

Five isoforms of acyl-CoA oxidase (Aox), designated Aox1p to Aox5p, constitute a 443-kD heteropentameric complex containing one polypeptide chain of each isoform within the peroxisomal matrix of the yeast Yarrowia lipolytica. Assembly of the Aox complex occurs in the cytosol and precedes its import into peroxisomes. Peroxisomal targeting of the Aox complex is abolished in a mutant lacking the p...

Journal: :The Biochemical journal 2001
L Amery H Sano G P Mannaerts J Snider J Van Looy M Fransen P P Van Veldhoven

Based on peroxin protein 5 (Pex5p) homology searches in the expressed sequence tag database and sequencing of large full-length cDNA inserts, three novel and related human cDNAs were identified. The brain-derived cDNAs coded for two related proteins that differ only slightly at their N-terminus, and exhibit 39.8% identity to human PEX5p. The shorter liver-derived cDNA coded for the C-terminal t...

2010
Naxhiely Martínez Ramón Bonnie Bartel

Peroxisomes compartmentalize certain metabolic reactions critical to plant and animal development. The import of proteins from the cytosol into the organelle matrix depends on more than a dozen peroxin (PEX) proteins, with PEX5 and PEX7 serving as receptors that shuttle proteins bearing one of two peroxisome-targeting signals (PTSs) into the organelle. PEX5 is the PTS1 receptor; PEX7 is the PTS...

Journal: :Plant physiology 2016
María Rodríguez-Serrano María C Romero-Puertas María Sanz-Fernández Jianping Hu Luisa M Sandalio

Peroxisomes are highly dynamic and metabolically active organelles that play an important role in cellular functions, including reactive oxygen species (ROS) metabolism. Peroxisomal dynamics, such as the proliferation, movement, and production of dynamic extensions called peroxules, have been associated with ROS in plant cells. However, the function and regulation of peroxules are largely unkno...

Journal: :Molecular & cellular proteomics : MCP 2013
Christine David Johannes Koch Silke Oeljeklaus Alexandra Laernsack Sophie Melchior Sebastian Wiese Andreas Schummer Ralf Erdmann Bettina Warscheid Cécile Brocard

Peroxisome biogenesis initiates at the endoplasmic reticulum (ER) and maturation allows for the formation of metabolically active organelles. Yet, peroxisomes can also multiply by growth and division. Several proteins, called peroxins, are known to participate in these processes but little is known about their organization to orchestrate peroxisome proliferation. Here, we demonstrate that regul...

Journal: :Plant physiology 2005
Jilian Fan Sheng Quan Travis Orth Chie Awai Joanne Chory Jianping Hu

Peroxisomes perform diverse and vital functions in eukaryotes, and abnormalities in peroxisomal function lead to severe developmental disorders in humans. Peroxisomes are also involved in a wide array of physiological and metabolic functions unique to plants, yet many aspects of this important organelle are poorly understood. In yeast and mammals, various steps in peroxisome biogenesis require ...

Journal: :The Journal of biological chemistry 2009
Robert Rucktäschel Sven Thoms Vadim Sidorovitch Andre Halbach Markos Pechlivanis Rudolf Volkmer Kirill Alexandrov Jürgen Kuhlmann Hanspeter Rottensteiner Ralf Erdmann

The conserved CaaX box peroxin Pex19p is known to be modified by farnesylation. The possible involvement of this lipid modification in peroxisome biogenesis, the degree to which Pex19p is farnesylated, and its molecular function are unknown or controversial. We resolve these issues by first showing that the complete pool of Pex19p is processed by farnesyltransferase in vivo and that this modifi...

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