Journal
MOLECULAR CELL
Volume 34, Issue 1, Pages 115-131Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2009.03.007
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Funding
- National Institutes of Health (NIH) [1301-CA1-18972, R01-CA126240]
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Melanoma and other cancers harbor oncogenic mutations in the protein kinase B-Raf, which leads to constitutive activation and dysregulation of MAP kinase signaling. In order to elucidate molecular determinants responsible for B-Raf control of cancer phenotypes, we present a method for phosphoprotein profiling, using negative ionization mass spectrometry to detect phosphopeptides based on their fragment ion signature caused by release of PO3-. The method provides an alternative strategy for phosphoproteomics, circumventing affinity enrichment of phosphopeptides and isotopic labeling of samples. Ninety phosphorylation events were regulated by oncogenic B-Raf signaling, based on their responses to treating melanoma cells with MKK1/2 inhibitor. Regulated phosphoproteins included known signaling effectors and cytoskeletal regulators. We investigated MINERVA/FAM129B, a target belonging to a protein family with unknown category and function,and established the importance of this protein and its; MAP kinase-dependent phosphorylation in controll'ing melanoma cell invasion into three-dimensional collagen matrix.
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