Glycoprotein capture and quantitative phosphoproteomics indicate coordinated regulation of cell migration upon lysophosphatidic acid stimulation.

Molecular & Cellular Proteomics : MCP
Nina MäusbacherHenrik Daub

Abstract

The lipid mediator lysophosphatidic acid (LPA) is a serum component that regulates cellular functions such as proliferation, migration, and survival via specific G protein-coupled receptors. The underlying signaling mechanisms are still incompletely understood, including those that operate at the plasma membrane to modulate cell-cell and cell-matrix interactions in LPA-promoted cell migration. To explore LPA-evoked phosphoregulation with a focus on cell surface proteins, we combined glycoproteome enrichment by immobilized lectins with SILAC-based quantitative phosphoproteomics. We performed biological replicate analyses in SCC-9 squamous cell carcinoma cells and repeatedly quantified the effect of 1.5- and 5-min LPA treatment on more than 700 distinct phosphorylations in lectin-purified proteins. We detected many regulated phosphorylation events on various types of plasma membrane proteins such as cell adhesion molecules constituting adherens junctions, desmosomes, and hemidesmosomes. Several of these LPA-regulated phosphorylation sites have been characterized in a biological context other than G protein-coupled receptor signaling, and the transfer of this functional information suggests coordinated and multifactorial cell adhe...Continue Reading

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Citations

Nov 2, 2014·Proceedings of the National Academy of Sciences of the United States of America·Hashem A DboukMelanie H Cobb
Jun 28, 2011·Electrophoresis·Marijana RucevicDjuro Josic
Jan 1, 2014·IEEE/ACM Transactions on Computational Biology and Bioinformatics·Fahad SaeedMark A Knepper
Nov 3, 2011·Analytical Chemistry·Carol L Nilsson
Dec 3, 2016·Proceedings of the National Academy of Sciences of the United States of America·Sachith Gallolu KankanamalageMelanie H Cobb

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