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Functional proteomics identifies targets of phosphorylation by B-Raf signaling in melanoma.

Abstract：

: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 PO(3)(-). 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 controlling melanoma cell invasion into three-dimensional collagen matrix.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Old WM,Shabb JB,Houel S,Wang H,Couts KL,Yen CY,Litman ES,Croy CH,Meyer-Arendt K,Miranda JG,Brown RA,Witze ES,Schweppe RE,Resing KA,Ahn NG

doi

10.1016/j.molcel.2009.03.007

subject

Has Abstract

pub_date

2009-04-10 00:00:00

pages

115-31

issue

1

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(09)00197-X

journal_volume

34

pub_type

杂志文章

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