HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 281, Issue 45, 34492-34502, November 10, 2006

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 281/45/34492    most recent M607183200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Pinto, M. P. Articles by Azevedo, J. E. Search for Related Content PubMed PubMed Citation Articles by Pinto, M. P. Articles by Azevedo, J. E. Social Bookmarking                      What's this?

The Import Competence of a Peroxisomal Membrane Protein Is Determined by Pex19p before the Docking Step^*

Manuel P. Pinto¹, Cláudia P. Grou¹, Inês S. Alencastre, Márcia E. Oliveira², Clara Sá-Miranda, Marc Fransen^¶, and Jorge E. Azevedo³

From the Instituto de Biologia Molecular e Celular (IBMC) Rua do Campo Alegre, 823, 4150-180 Porto, Portugal, the Instituto de Ciências Biomédicas de Abel Salazar (ICBAS), Universidade do Porto, Largo do Professor Abel Salazar, 2, 4099-003 Porto, Portugal, and the ^¶Katholieke Universiteit Leuven, Faculteit Geneeskunde, Departement Moleculaire Celbiologie, Herestraat 49, B-3000 Leuven, Belgium

Biogenesis of the mammalian peroxisomal membrane requires the action of Pex3p and Pex16p, two proteins present in the organelle membrane, and Pex19p, a protein that displays a dual subcellular distribution (peroxisomal and cytosolic). Pex19p interacts with most peroxisomal intrinsic membrane proteins, but whether this property reflects its role as an import receptor for this class of proteins or a chaperone-like function in the assembly/disassembly of peroxisomal membrane proteins has been the subject of much controversy. Here, we describe an in vitro system particularly suited to address this issue. It is shown that insertion of a reporter protein into the peroxisomal membrane is a Pex3p-dependent process that does not require ATP/GTP hydrolysis. The system can be programmed with recombinant versions of Pex19p, allowing us to demonstrate that Pex19p-cargo protein complexes formed in the absence of peroxisomes are the substrates for the peroxisomal docking/insertion machinery. Data suggesting that cargo-loaded Pex19p displays a much higher affinity for Pex3p than Pex19p alone are also provided. These results suggest that soluble Pex19p participates in the targeting of newly synthesized peroxisomal membrane proteins to the organelle membrane and support the existence of a cargo-induced peroxisomal targeting mechanism for Pex19p.

Received for publication, July 28, 2006 , and in revised form, September 6, 2006.

^* The work done in Porto was supported by Fundação para a Ciência e Tecnologia Grant POCTI2010 and Fundo Europeu de Desenvolvimento Regional (FEDER) Funds, Portugal, and by European Union VI Framework program Grant LSHG-CT-2004-512018, Peroxisomes in Health and Disease. The work done in Leuven was supported by the Flemish Government (Geconcerteerde Onderzoeksacties Grant GOA/2004/08) and Fonds voor Wetenschappelijk Onderzoek Vlaanderen (Onderzoeksproject Grant G.0237.04). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. 1S and 2S.

¹ Supported by Fundação para a Ciência e Tecnologia.

² Present address: Instituto de Genética Médica Jacinto Magalhães, Praça Pedro Nunes, 4050-466 Porto, Portugal.

³ To whom correspondence should be addressed: Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal. Tel.: 351-226074900; Fax: 351-226099157; E-mail: jazevedo{at}ibmc.up.pt.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				B. H. Welter and L. A. Temesvari Overexpression of a Mutant Form of EhRabA, a Unique Rab GTPase of Entamoeba histolytica, Alters Endoplasmic Reticulum Morphology and Localization of the Gal/GalNAc Adherence Lectin Eukaryot. Cell, July 1, 2009; 8(7): 1014 - 1026. [Abstract] [Full Text] [PDF]

				A. Halbach, R. Rucktaschel, H. Rottensteiner, and R. Erdmann The N-domain of Pex22p Can Functionally Replace the Pex3p N-domain in Targeting and Peroxisome Formation J. Biol. Chem., February 6, 2009; 284(6): 3906 - 3916. [Abstract] [Full Text] [PDF]

				J. M. Fletcher, M. A. Jordan, S. L. Snelgrove, R. M. Slattery, F. D. Dufour, K. Kyparissoudis, G. S. Besra, D. I. Godfrey, and A. G. Baxter Congenic Analysis of the NKT Cell Control Gene Nkt2 Implicates the Peroxisomal Protein Pxmp4 J. Immunol., September 1, 2008; 181(5): 3400 - 3412. [Abstract] [Full Text] [PDF]

				Y. Sato, H. Shibata, H. Nakano, Y. Matsuzono, Y. Kashiwayama, Y. Kobayashi, Y. Fujiki, T. Imanaka, and H. Kato Characterization of the Interaction between Recombinant Human Peroxin Pex3p and Pex19p: IDENTIFICATION OF TRP-104 IN Pex3p AS A CRITICAL RESIDUE FOR THE INTERACTION J. Biol. Chem., March 7, 2008; 283(10): 6136 - 6144. [Abstract] [Full Text] [PDF]

				T. Saveria, A. Halbach, R. Erdmann, R. Volkmer-Engert, C. Landgraf, H. Rottensteiner, and M. Parsons Conservation of PEX19-Binding Motifs Required for Protein Targeting to Mammalian Peroxisomal and Trypanosome Glycosomal Membranes Eukaryot. Cell, August 1, 2007; 6(8): 1439 - 1449. [Abstract] [Full Text] [PDF]