Generic placeholder image

Current Protein & Peptide Science

Editor-in-Chief

ISSN (Print): 1389-2037
ISSN (Online): 1875-5550

Molecular Mechanism of P-glycoprotein Assembly into Cellular Membranes

Author(s): Victoria Anthony and William R. Skach

Volume 3, Issue 5, 2002

Page: [485 - 501] Pages: 17

DOI: 10.2174/1389203023380503

Price: $65

Abstract

In the past decade major advances have been made towards understanding the mechanisms by which polytopic membrane proteins fold and assemble in cellular membranes. In eukaryotes, this process is mediated by a complex set of machinery in the endoplasmic reticulum (ER) that facilitates translocation of peptide loops across and integration of hydrophobic helices into the lipid bilayer. Studies evaluating the biogenesis of P-glycoprotein (P-gp) have been at the forefront of this rapidly expanding field. They have revealed a fascinating although sometimes confusing picture that has challenged our notions about general mechanisms of polytopic protein assembly and questioned specific predictions about the details and uniqueness of P-gp transmembrane topology. This review will attempt to summarize and consolidate our current knowledge of the sequence of events that gives rise to P-gp topology in the ER compartment and the implications of these events for polytopic protein biogenesis and function.

Keywords: P-glycoprotein, Cellular Membranes, TOPOLOGY, BIOGENESIS

Next »

Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy