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Am J Physiol Renal Physiol 283: F663-F670, 2002. First published May 7, 2002; doi:10.1152/ajprenal.00338.2001
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Vol. 283, Issue 4, F663-F670, October 2002

A central role for Pyk2-Src interaction in coupling diverse stimuli to increased epithelial NBC activity

Doris Joy D. Espiritu1,2, Angelito A. Bernardo1,2, R. Brooks Robey1,2,3, and Jose A. L. Arruda1,2,3

1 Section of Nephrology, Department of Medicine, University of Illinois at Chicago, Chicago 60612 - 7315; 3 Department of Physiology and Biophysics, College of Medicine, University of Illinois at Chicago, Chicago 60612 - 7342; and 2 West Side Division, Veterans Administration Chicago Health Care System, Chicago, Illinois 60612

Regulation of renal Na-HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> cotransporter (NBC1) activity by cholinergic agonists, ANG II, and acute acidosis (CO2) requires both Src family kinase (SFK) and classic MAPK pathway activation. The nonreceptor tyrosine kinase proline-rich tyrosine kinase 2 (Pyk2) couples discrete G protein-coupled receptor and growth factor receptor signaling to SFK activation. We examined the role of Pyk2-SFK interaction in coupling these stimuli to increased NBC1 activity in opossum kidney cells. Carbachol increased tyrosine autophosphorylation of endogenous Pyk2 and ectopically expressed wild-type Pyk2 and were abrogated by kinase-dead mutant (Pyk2-KD) overexpression. Pyk2 phosphorylation was calcium/calmodulin dependent, and Pyk2 associated with Src by means of SH2 domain interaction. Pyk2 phosphorylation and Pyk2-Src interaction by carbachol were mimicked by both ANG II and CO2. To correlate Pyk2 autophosphorylation and Pyk2-Src interaction with NBC activity, cotransporter activity was measured in untransfected cells and in cells overexpressing Pyk2-KD in the presence or absence of carbachol, ANG II, or CO2. In Pyk2-KD-overexpressing cells, the effect of carbachol, ANG II, and CO2 was abolished. We conclude that Pyk2 plays a central role in coupling carbachol, ANG II, and CO2 to increased NBC activity. This coupling is mediated by Pyk2 autophosphorylation and Pyk2-Src interaction.

carbachol; angiotensin II; acute acidosis; autophosphorylation; sodium-bicarbonate cotransporter; proline-rich tyrosine kinase 2


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