Open AccessMitogen-Activated Protein Kinase Activation Is Insufficient for Growth Factor Receptor-Mediated PC12 Cell Differentiation
Author(s) -
Richard R. Vaillancourt,
Lynn E. Heasley,
Jeffrey Zamarripa,
Brooke Storey,
Mindaugas Valius,
Andrius Kazlauskas,
Gary L. Johnson
Publication year - 1995
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.15.7.3644
Subject(s) - biology , platelet derived growth factor receptor , microbiology and biotechnology , receptor tyrosine kinase , growth factor receptor , map kinase kinase kinase , c raf , mitogen activated protein kinase kinase , ask1 , mitogen activated protein kinase , cellular differentiation , signal transduction , growth factor , mapk/erk pathway , receptor , biochemistry , protein kinase c , gene
When expressed in PC12 cells, the platelet-derived growth factor beta receptor (beta PDGF-R) mediates cell differentiation. Mutational analysis of the beta PDGF-R indicated that persistent receptor stimulation of the Ras/Raf/mitogen-activated protein (MAP) kinase pathway alone was insufficient to sustain PC12 cell differentiation. PDGF receptor activation of signal pathways involving p60c-src or the persistent regulation of phospholipase C gamma was required for PC12 cell differentiation. beta PDGF-R regulation of phosphatidylinositol 3-kinase, the GTPase-activating protein of Ras, and the tyrosine phosphatase, Syp, was not required for PC12 cell differentiation. In contrast to overexpression of oncoproteins involved in regulating the MAP kinase pathway, growth factor receptor-mediated differentiation of PC12 cells requires the integration of other signals with the Ras/Raf/MAP kinase pathway.
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