Phosphorylation of Shc by Src family kinases is necessary for stem cell factor receptor/c-kit mediated activation of the Ras/MAP kinase pathway and c-fos induction (Q28145948)

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scientific article (publication date: 30 September 1999)

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English	Phosphorylation of Shc by Src family kinases is necessary for stem cell factor receptor/c-kit mediated activation of the Ras/MAP kinase pathway and c-fos induction	scientific article (publication date: 30 September 1999)

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scholarly article

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Phosphorylation of Shc by Src family kinases is necessary for stem cell factor receptor/c-kit mediated activation of the Ras/MAP kinase pathway and c-fos induction (English)

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phosphorylation

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author name string

J Lennartsson

1

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P Blume-Jensen

2

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M Hermanson

3

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E Pontén

4

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M Carlberg

5

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L Rönnstrand

6

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language of work or name

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publication date

30 September 1999

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18

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40

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5546-53

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Myc but not Fos rescue of PDGF signalling block caused by kinase-inactive Src.

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Identification of the major phosphorylation sites for protein kinase C in kit/stem cell factor receptor in vitro and in intact cells

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From white spots to stem cells: the role of the Kit receptor in mammalian development

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c-Kit-kinase induces a cascade of protein tyrosine phosphorylation in normal human melanocytes in response to mast cell growth factor and stimulates mitogen-activated protein kinase but is down-regulated in melanomas

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Gain-of-function mutations of c-kit in human gastrointestinal stromal tumors

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SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain

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Association between the PDGF receptor and members of the src family of tyrosine kinases

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Protein modules and signalling networks

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Kit signaling through PI 3-kinase and Src kinase pathways: an essential role for Rac1 and JNK activation in mast cell proliferation

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Characterization of the polypeptide composition of human factor VIII:C and the nucleotide sequence and expression of the human kidney cDNA.

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The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions

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Steel locus defines new multipotent growth factor

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Increased Kit/SCF receptor induced mitogenicity but abolished cell motility after inhibition of protein kinase C.

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ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation

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A specific combination of substrates is involved in signal transduction by the kit-encoded receptor.

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A platelet factor that stimulates the proliferation of vascular endothelial cells

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Identifiers

10.1038/SJ.ONC.1202929

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

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Springer Nature article ID

10.1038/sj.onc.1202929

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