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Native mass spectrometry reveals the simultaneous binding of lipids and zinc to rhodopsin

Authors
  • Norris, Carolanne E.1
  • Keener, James E.1
  • Perera, Suchithranga M.D.C.1
  • Nipuna Weerasinghe1
  • Fried, Steven D.E.1
  • Resager, William C.1
  • Rohrbough, James G.1
  • Brown, Michael F.1, 2, 3
  • Marty, Michael T.1, 3
Type
Published Article
Journal
International Journal of Mass Spectrometry
Publisher
Elsevier BV
Publication Date
Mar 03, 2021
Volume
460
Identifiers
DOI: 10.1016/j.ijms.2020.116477
Source
MyScienceWork
License
White

Abstract

Rhodopsin, a prototypical G-protein-coupled receptor, is responsible for scoptic vision at low-light levels. Although rhodopsin’s photoactivation cascade is well understood, it remains unclear how lipid and zinc binding to the receptor are coupled. Using native mass spectrometry, we developed a novel data analysis strategy to deconvolve zinc and lipid bound to the proteoforms of rhodopsin and investigated the allosteric interaction between lipids and zinc binding. We discovered that phosphatidylcholine bound to rhodopsin with a greater affinity than phosphatidylserine or phosphatidylethanolamine, and that binding of all lipids was influenced by zinc but with different effects. In contrast, zinc binding was relatively unperturbed by lipids. Overall, these data reveal that lipid binding can be strongly and differentially influenced by metal ions.

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