Mouse liver PMP70 and ALDP: homomeric interactions prevail in vivo

• Type: Article in International Scientific Journal
• Date: 2004

Authors

guimaraes, cp (Author) Other; domingues, p (Author) Other; aubourg, p (Author) Other; fouquet, f (Author) Other; pujol, a (Author) Other; jimenez-sanchez, g (Author) Other; sa-miranda, c (Author) Other; azevedo, je (Author) ICBAS

Journal

Title: Biochimica et Biophysica Acta - Molecular Basis of Disease

Vol. 1689

Pages: 235-243

ISSN: 0925-4439

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 34 Citations

Scopus - 34 Citations

Other information

Authenticus ID: P-000-91A

DOI: 10.1016/j.bbadis.2004.04.001

Abstract (EN): ALDP, ALDPR, PMP70 and PMP70R are half ATP-binding cassette (ABC) transporters of the mammalian peroxisomal membrane. By analogy with other members of this family, it is assumed that peroxisomal ABC transporters must dimerize to become functional units. However, not much is known regarding the type of dimers (i.e., homodimers and/or heterodimers) that are formed in vivo under normal expression conditions. In this work, we have characterized the quaternary structure of mouse liver PMP70 and ALDR The PMP70 protein complex was purified to apparent homogeneity using a two-step purification protocol. The ALDP-containing protein complex was characterized by preparative immunoprecipitation experiments. In both cases, no evidence for the existence of heteromeric interactions or for the presence of accessory proteins in these ABC transporter protein complexes could be obtained. Our data indicate that the majority (if not all) of mouse liver PMT70 and ALDP are homomeric proteins. (C) 2004 Elsevier B.V. All rights reserved.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 9