Journal
NATURE COMMUNICATIONS
Volume 8, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-017-01461-z
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Funding
- Focus & Massa: Life Sciences and Biocomplexity grant from the Utrecht University
- Council for Chemical Sciences of the Netherlands Organization for Scientific Research (NWO-CW) grant Targeting Membrane Proteins [731.015.201]
- Proteins At Work, a program of the Netherlands Proteomics Centre - NWO as part of the National Roadmap Large-scale Research Facilities of the Netherlands [184.032.201]
- Fundamenteel Onderzoek der Materie (FOM) [12PR3303-2]
- Institute for Chemical Immunology, an NWO Gravitation project - Ministry of Education, Culture and Science of the Netherlands
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Palmitoylation affects membrane partitioning, trafficking and activities of membrane proteins. However, how specificity of palmitoylation and multiple palmitoylations in membrane proteins are determined is not well understood. Here, we profile palmitoylation states of three human claudins, human CD20 and cysteine-engineered prokaryotic KcsA and bacteriorhodopsin by native mass spectrometry. Cysteine scanning of claudin-3, KcsA, and bacteriorhodopsin shows that palmitoylation is independent of a sequence motif. Palmitoylations are observed for cysteines exposed on the protein surface and situated up to 8 angstrom into the inner leaflet of the membrane. Palmitoylation on multiple sites in claudin-3 and CD20 occurs stochastically, giving rise to a distribution of palmitoylated membrane-protein isoforms. Non-native sites in claudin-3 indicate that membrane-protein function imposed evolutionary restraints on native palmitoylation sites. These results suggest a generic, stochastic membrane-protein palmitoylation process that is determined by the accessibility of palmitoyl-acyl transferases to cysteines on membrane-embedded proteins, and not by a preferred substrate-sequence motif.
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