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PMID: 22352709 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Rhodopsin forms a dimer with cytoplasmic helix 8 contacts in native membranes.

Biochemistry ·Vol. 51 ·No. 9 ·2012-03-06 ·Pages 1819-21

Knepp AM, Periole X, Marrink SJ, Sakmar TP, Huber T

Abstract

G protein-coupled receptors form dimers and higher-order oligomers in membranes, but the precise mode of receptor-receptor interaction remains unknown. To probe the intradimeric proximity of helix 8 (H8), we conducted chemical cross-linking of endogenous cysteines in rhodopsin in disk membranes. We identified a Cys316-Cys316 cross-link using partial proteolysis and liquid chromatography with mass spectrometry. These results show that a symmetric dimer interface mediated by H1 and H8 contacts is present in native membranes.

MeSH Terms
Binding Sites Cell Membrane/metabolism Chromatography, Liquid Cysteine/chemistry,genetics Cytoplasm/metabolism Dimerization Mass Spectrometry Protein Structure, Secondary Proteolysis Rhodopsin/chemistry,metabolism
Chemicals
Rhodopsin Cysteine
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Knepp Adam M
Laboratory of Molecular Biology and Biochemistry, The Rockefeller University, New York, New York 10065, United States.
Periole Xavier
Marrink Siewert-Jan
Sakmar Thomas P
Huber Thomas
References (9)
9 references, click to expand
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Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
1520-4995
DOI
10.1021/bi3001598
Published
2012-03-06
Epub
2012-00-27
Pages
1819-21
Language
English
Region
United States
NLM ID
0370623
PMCID
PMC3332060
Subset
IM
Grants
NEI NIH HHS · R01 EY012049 · United States
NEI NIH HHS · R01 EY012049-12 · United States
External Links
PubMed source DOI: 10.1021/bi3001598 PMC Full Text View journal details
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