Abstract:
: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 stable isotope labeling by amino acids in cell culture-mass spectrometry, we profiled the phosphoproteomic changes induced by the interactions of cell integrins with type I collagen, the most common ECM substratum. Integrin-ECM interactions modulate phosphorylation of 517 serine, threonine, or tyrosine residues in 513 peptides, corresponding to 357 proteins. Among these proteins, 33 key signaling mediators with kinase or phosphatase activity were subjected to small interfering RNA-based functional screening. Three integrin-regulated kinases, DBF4, PAK2, and GRK6, were identified for their critical role in cell adhesion and migration possibly through their regulation of actin cytoskeleton arrangement. Altogether, we not only depict an integrin-modulated phosphorylation network during cell-ECM protein interactions but also reveal novel regulators for cell adhesion and migration.
journal_name
Cancer Resjournal_title
Cancer researchauthors
Chen Y,Lu B,Yang Q,Fearns C,Yates JR 3rd,Lee JDdoi
10.1158/0008-5472.CAN-08-2515subject
Has Abstractpub_date
2009-04-15 00:00:00pages
3713-20issue
8eissn
0008-5472issn
1538-7445pii
0008-5472.CAN-08-2515journal_volume
69pub_type
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