 | Na,K-ATPase AND RELATED CATION PUMPS: Structure, Function, and Regulatory Mechanisms
Copyright © 2003 by the New York Academy of Sciences
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Annals of the New York Academy of Sciences 986:360-368 (2003)
© 2003 New York Academy of Sciences
Ion Pump-Interacting Proteins: Promising New Partners
PHILIPP PAGEL,
ALESSANDRA ZATTI,
TOHRU KIMURA,
AMY DUFFIELD,
VERONIQUE CHAUVET,
VANATHY RAJENDRAN AND
MICHAEL J. CAPLAN
Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06510, USA
Address for correspondence: Michael J. Caplan, Department of Cellular and Molecular Physiology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510. Voice: 203-785-7316; fax: 203-785-4951.
Michael.caplan{at}yale.edu
Ann. N.Y. Acad. Sci. 986: 360-368 (2003).
The sorting and regulation of the Na,K and H,K-ATPases requires that the pump proteins must associate, at least transiently, with kinases, phosphatases, scaffolding molecules, and components of the cellular trafficking machinery. The identities of these interacting proteins and the nature of their associations with the pump polypeptides have yet to be elucidated. We have begun a series of yeast two-hybrid screens employing structurally defined segments of pump polypeptides as baits in order to gain insight into the nature and function of these interacting proteins.
Key Words: ion pumps • interactions • tetraspan • polycystin • two hybrid
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