Probing substrate-induced conformational alterations in adrenoleukodystrophy protein by proteolysis

• Type: Article in International Scientific Journal
• Date: 2005

Authors

guimaraes, cp (Author) Other; sa-miranda, c (Author) Other; azevedo, je (Author) ICBAS

Journal

Title: Journal of Human Genetics

Vol. 50

Pages: 99-105

ISSN: 1434-5161

Publisher: Springer Nature

Indexing

ISI Web of Knowledge - 10 Citations

Scopus - 10 Citations

Other information

Authenticus ID: P-000-4WY

DOI: 10.1007/s10038-004-0226-4

Abstract (EN): The adrenoleukodystrophy protein (ALDP) is a half-ABC (ATP-binding cassette) transporter localized in the peroxisomal membrane. Dysfunction of this protein is the cause of the human genetic disorder X-linked adrenoleukodystrophy (X-ALD), which is characterized by accumulation of saturated, very-long-chain fatty acids (VLCFAs). This observation suggests that ALDP is involved in the metabolism of these compounds. Whether ALDP transports VLCFAs or their derivatives across the peroxisomal membrane or some cofactors essential for the efficient peroxisomal b-oxidation of these fatty acids is still unknown. In this work, we used a protease-based approach to search for substrate-induced conformational alterations on ALDP. Our results suggest that ALDP is directly involved in the transport of long- and very-long-chain acyl-CoAs across the peroxisomal membrane.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 7