185 341

Cited 22 times in

Lipid raft proteome reveals that oxidative phosphorylation system is associated with the plasma membrane.

Authors
Kim, BW; Lee, CS; Yi, JS; Lee, JH; Lee, JW; Choo, HJ; Jung, SY; Kim, MS; Lee, SW; Lee, MS; Yoon, G; Ko, YG
Citation
Expert review of proteomics, 7(6):849-866, 2010
Journal Title
Expert review of proteomics
ISSN
1478-94501744-8387
Abstract
Although accumulating proteomic analyses have supported the fact that mitochondrial oxidative phosphorylation (OXPHOS) complexes are localized in lipid rafts, which mediate cell signaling, immune response and host-pathogen interactions, there has been no in-depth study of the physiological functions of lipid-raft OXPHOS complexes. Here, we show that many subunits of OXPHOS complexes were identified from the lipid rafts of human adipocytes, C2C12 myotubes, Jurkat cells and surface biotin-labeled Jurkat cells via shotgun proteomic analysis. We discuss the findings of OXPHOS complexes in lipid rafts, the role of the surface ATP synthase complex as a receptor for various ligands and extracellular superoxide generation by plasma membrane oxidative phosphorylation complexes.
MeSH terms
ATP Synthetase Complexes/metabolismAdenosine Triphosphate/biosynthesisAnimalsCell Membrane/enzymology*HumansMembrane Microdomains/enzymology*MiceMitochondrial Membranes/enzymologyMultienzyme Complexes/metabolism*Oxidative PhosphorylationProteome/metabolism*Superoxides/metabolism
DOI
10.1586/epr.10.87
PMID
21142887
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Biochemistry & Molecular Biology
AJOU Authors
윤계순
Full Text Link
Files in This Item:
Full-Text Not Available.txtDownload
Export
RIS (EndNote)
XLS (Excel)
XML

qrcode

해당 아이템을 이메일로 공유하기 원하시면 인증을 거치시기 바랍니다.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse