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Articles in PresS, published online ahead of print May 7, 2002
Am J Physiol Renal Physiol, 10.1152/ajprenal.00338.2001
Submitted on November 9, 2001
Accepted on April 30, 2002
1 Department of Medicine, Section of Nephrology, University of Illinois at Chicago, Chicago, IL, USA; West Side Division, VA Chicago Health Care System, Chicago, IL, USA
2 Department of Medicine, Section of Nephrology, University of Illinois at Chicago, Chicago, IL, USA; Department of Physiology & Biophysics, College of Medicine, University of Illinois at Chicago, Chicago, IL, USA; West Side Division, VA Chicago Health Care System, Chicago, IL, USA
* To whom correspondence should be addressed. E-mail: JAArruda{at}uic.edu.
Regulation of the renal Na/HCO3 cotransport (NBC1) activity by cholinergic agonists, angiotensin II (AII), and acute acidosis (CO2) require both Src family kinase (SFK) and classic MAPK pathway activation. The non-receptor tyrosine kinase, 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 OK cells. Carbachol increased tyrosine autophosphorylation of endogenous PYK2 and ectopically expressed wild-type Pyk2 (PYK2-WT), and were abrogated by kinase-dead mutant (PYK2-KD) overexpression. Pyk2 phosphorylation was Ca2+/calmodulin-dependent and Pyk2 associate with Src via Src homology 2 (SH2) domain interaction. Pyk2 phosphorylation and Pyk2-Src interaction by carbachol were mimicked by both AII and CO2. To correlate Pyk2 autophosphorylation and Pyk2/Src interaction with NBC activity, cotransporter activity was measured in unstransfected cells and in cells overexpressing PYK2-KD, in the presence or absence of carbachol, AII or CO2. In PYK2-KD overexpressing cells, the effect of carbachol, AII and CO2 was abolished. We conclude that Pyk2 plays a central role in coupling carbachol, AII and CO2 to increased NBC activity. This coupling is mediated by Pyk2 autophosphorylation and Pyk2-Src interaction.
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