INTEGRIN PHOSPHOPROTEOMICS IDENTIFIED KEY KINASES

University Of Washington, Seattle WA

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Abstract

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Integrins interact with extracellular matrix (ECM) and deliver intracellular signaling for cell proliferation, survival and motility. During tumor metastasis, integrin-mediated cell adhesion to and migration on the ECM proteins are required for cancer cell survival and adaptation to the new microenvironment. Using SILAC-MS (Stable-Isotope Labeling by Amino acids in Cell culture-Mass Spectrometry), we profiled the phosphoproteomic changes induced by the interaction of cell integrins with type I collagen, the most common ECM substratum. We not only depict an integrin-modulated phosphorylation network during cell-ECM protein interactions but also reveal novel regulators for cell adhesion and migration.