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The protein phosphatase 2A regulatory subunits B'beta and B'delta mediate sustained TrkA neurotrophin receptor autophosphorylation and neuronal differentiation
Journal article   Peer reviewed

The protein phosphatase 2A regulatory subunits B'beta and B'delta mediate sustained TrkA neurotrophin receptor autophosphorylation and neuronal differentiation

Michael J Van Kanegan and Stefan Strack
Molecular and cellular biology, Vol.29(3), pp.662-674
02/2009
DOI: 10.1128/MCB.01242-08
PMCID: PMC2630673
PMID: 19029245

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Abstract

Nerve growth factor (NGF) is critical for the differentiation and maintenance of neurons in the peripheral and central nervous system. Sustained autophosphorylation of the TrkA receptor tyrosine kinase and long-lasting activation of downstream kinase cascades are hallmarks of NGF signaling, yet our knowledge of the molecular mechanisms underlying prolonged TrkA activity is incomplete. Protein phosphatase 2A (PP2A) is a heterotrimeric Ser/Thr phosphatase composed of a scaffolding, catalytic, and regulatory subunit (B, B', and B" gene families). Here, we employ a combination of pharmacological inhibitors, regulatory subunit overexpression, PP2A scaffold subunit exchange, and RNA interference to show that PP2A containing B' family regulatory subunits participates in sustained NGF signaling in PC12 cells. Specifically, two neuron-enriched regulatory subunits, B'beta and B'delta, recruit PP2A into a complex with TrkA to dephosphorylate the NGF receptor on Ser/Thr residues and to potentiate its intrinsic Tyr kinase activity. Acting at the receptor level, PP2A/ B'beta and B'delta enhance NGF (but not epidermal growth factor or fibroblast growth factor) signaling through the Akt and Ras-mitogen-activated protein kinase cascades and promote neuritogenesis and differentiation of PC12 cells. Thus, select PP2A heterotrimers oppose desensitization of the TrkA receptor tyrosine kinase, perhaps through dephosphorylation of inhibitory Ser/Thr phosphorylation sites on the receptor itself, to maintain neurotrophin-mediated developmental and survival signaling.
Humans Neurites - enzymology Male Neurons - cytology PC12 Cells Protein Subunits - metabolism Phosphorylation - drug effects Neurons - drug effects Neurites - drug effects Protein Phosphatase 2 - antagonists & inhibitors Mice, Inbred C57BL Enzyme Inhibitors - pharmacology Nerve Growth Factor - pharmacology Rats Enzyme Activation - drug effects Phosphoserine - metabolism Phosphothreonine - metabolism Animals Receptor, trkA - metabolism Cell Differentiation - drug effects Neurons - enzymology Protein Phosphatase 2 - metabolism Mice Cell Cycle - drug effects Mitogen-Activated Protein Kinases - metabolism

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