MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fransen, M.
Right arrow Articles by Van Veldhoven, P. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fransen, M.
Right arrow Articles by Van Veldhoven, P. P.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, July 2001, p. 4413-4424, Vol. 21, No. 13
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.13.4413-4424.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Human Pex19p Binds Peroxisomal Integral Membrane Proteins at Regions Distinct from Their Sorting Sequences

Marc Fransen,* Tine Wylin, Chantal Brees, Guy P. Mannaerts, and Paul P. Van Veldhoven*

Katholieke Universiteit Leuven, Campus Gasthuisberg (O/N), Departement Moleculaire Celbiologie, Afdeling Farmacologie, B-3000 Leuven, Belgium

Received 10 January 2001/Returned for modification 13 February 2001/Accepted 10 April 2001

The molecular machinery underlying peroxisomal membrane biogenesis is not well understood. The observation that cells deficient in the peroxins Pex3p, Pex16p, and Pex19p lack peroxisomal membrane structures suggests that these molecules are involved in the initial stages of peroxisomal membrane formation. Pex19p, a predominantly cytosolic protein that can be farnesylated, binds multiple peroxisomal integral membrane proteins, and it has been suggested that it functions as a soluble receptor for the targeting of peroxisomal membrane proteins (PMPs) to the peroxisome. An alternative view proposes that Pex19p functions as a chaperone at the peroxisomal membrane. Here, we show that the peroxisomal sorting determinants and the Pex19p-binding domains of a number of PMPs are distinct entities. In addition, we extend the list of peroxins with which human Pex19p interacts to include the PMP Pex16p and show that Pex19p's CaaX prenylation motif is an important determinant in the affinity of Pex19p for Pex10p, Pex11pbeta , Pex12p, and Pex13p.


* Corresponding author. Mailing address for Marc Fransen: Katholieke Universiteit Leuven, Campus Gasthuisberg (O/N), Departement Moleculaire Celbiologie, Afdeling Farmacologie, Herestraat 49, B-3000 Leuven, Belgium. Phone: 32-16-345786. Fax: 32-16-345699. E-mail: marc.fransen{at}med.kuleuven.ac.be. Mailing address for Paul P. Van Veldhoven: Katholieke Universiteit Leuven, Campus Gasthuisberg (O/N), Departement Moleculaire Celbiologie, Afdeling Farmacologie, Herestraat 49, B-3000 Leuven, Belgium. Phone: 32-16-345802. Fax: 32-16-345699. E-mail: paul.vanveldhoven{at}med.kuleuven.ac.be.


Molecular and Cellular Biology, July 2001, p. 4413-4424, Vol. 21, No. 13
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.13.4413-4424.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2001 by the American Society for Microbiology. All rights reserved.