Molecular mechanism of P-glycoprotein assembly into cellular membranes

Victoria Anthony, William Skach

Research output: Contribution to journalArticle

24 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)485-501
Number of pages17
JournalCurrent Protein and Peptide Science
Volume3
Issue number5
DOIs
StatePublished - Oct 2002

Fingerprint

P-Glycoprotein
Membranes
Endoplasmic Reticulum
Topology
Lipid bilayers
Lipid Bilayers
Eukaryota
Machinery
Membrane Proteins
Proteins
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Molecular mechanism of P-glycoprotein assembly into cellular membranes. / Anthony, Victoria; Skach, William.

In: Current Protein and Peptide Science, Vol. 3, No. 5, 10.2002, p. 485-501.

Research output: Contribution to journalArticle

Anthony, Victoria ; Skach, William. / Molecular mechanism of P-glycoprotein assembly into cellular membranes. In: Current Protein and Peptide Science. 2002 ; Vol. 3, No. 5. pp. 485-501.
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