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• W2147554431 abstract "<strong>Background:</strong> Spatio-temporal control of extracellular signal-regulated kinase (ERK) activity, a critical determinant of the cell's response to growth factors, requires timely dephosphorylation of its regulatory tyrosine and/or threonine residue by MAPK phosphatases. We studied the physiological role of kinase interaction motif (KIM)-containing protein tyrosine phosphatases (PTPs) in the control of EGF- and NGF-induced ERK activity in neuroendocrine PC12 cells. <strong>Results:</strong> We found a single KIM-containing PTP to be endogenously expressed in rat PC12 cells: the transmembrane PTPRR isoform termed PCPTP1. Protein knock-down of PCPTP1, or fourfold overexpression of its mouse orthologue, PTPBR7, left EGF- and NGF-induced ERK1/2 activity in PC12 cells unaltered. Ectopic expression of cytosolic PTPRR isoforms, however, resulted in reduced EGF-induced ERK1/2 activity, an effect that was dependent on the phosphatase activity and the KIM-domain of these PTPs. <strong>Conclusion:</strong> The finding that robust changes in tyrosine-specific MAPK phosphatase expression levels have minor effects on temporal ERK1/2 activity control in PC12 cells suggests that dualspecificity MAPK phosphatases may act as major regulators of growth factor-induced ERK1/2 signaling in these cells." @default.
• W2147554431 created "2016-06-24" @default.
• W2147554431 creator A5047261726 @default.
• W2147554431 creator A5079615023 @default.
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• W2147554431 date "2006-11-29" @default.
• W2147554431 modified "2023-10-03" @default.
• W2147554431 title "Tyrosine-specific MAPK phosphatases and the control of ERK signaling in PC12 cells" @default.
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• W2147554431 doi "https://doi.org/10.1186/1750-2187-1-4" @default.
• W2147554431 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1761141" @default.
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