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J Biol Chem, Vol. 274, Issue 12, 8093-8102, March 19, 1999
From the The signaling pathways by which cell volume
regulates ion transporters, e.g.
Na+/H+ exchangers (NHEs), and affects
cytoskeletal organization are poorly understood. We have previously
shown that shrinkage induces tyrosine phosphorylation in CHO cells,
predominantly in an 85-kDa band. To identify volume-sensitive kinases
and their substrates, we investigated the effect of hypertonicity on
members of the Src kinase family. Hyperosmolarity stimulated Fyn and
inhibited Src. Fyn activation was also observed in
nystatin-permeabilized cells, where shrinkage cannot induce
intracellular alkalinization. In contrast, osmotic inhibition of Src
was prevented by permeabilization or by inhibiting NHE-1. PP1, a
selective Src family inhibitor, strongly reduced the
hypertonicity-induced tyrosine phosphorylation. We identified one of
the major targets of the osmotic stress-elicited phosphorylation as
cortactin, an 85-kDa actin-binding protein and well known Src family
substrate. Cortactin phosphorylation was triggered by shrinkage and not
by changes in osmolarity or pHi and was abrogated by PP1.
Hyperosmotic cortactin phosphorylation was reduced in Fyn-deficient
fibroblasts but remained intact in Src-deficient fibroblasts. To
address the potential role of the Src family in the osmotic regulation
of NHEs, we used PP1. The drug affected neither the hyperosmotic
stimulation of NHE-1 nor the inhibition of NHE-3. Thus, members of the
Src family are volume-sensitive enzymes that may participate in the
shrinkage-related reorganization of the cytoskeleton but are probably
not responsible for the osmotic regulation of NHE.
Cell Shrinkage Regulates Src Kinases and Induces Tyrosine
Phosphorylation of Cortactin, Independent of the Osmotic Regulation of
Na+/H+ Exchangers
,,, and
Department of Surgery, The Toronto Hospital
and University of Toronto, Toronto, Ontario M5G 1L7, Canada and the
¶ Department of Physiology and Laboratory of Cellular and
Molecular Physiology, Semmelweis University of Medicine, Budapest 8, P.O. Box 259, H-1444 Budapest, Hungary
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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