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Vol. 273, Issue 3, 1273-1276, January 16, 1998
From the Molecular Neurogenetics Unit, Massachusetts General
Hospital, Charlestown, Massachusetts 02129 and the ¶ Center for
Cancer Research, Massachusetts Institute of Technology, Cambridge,
Massachusetts 02139
We have identified the human homologue of a
regulatory cofactor of Na+-H+ exchanger
(NHE-RF) as a novel interactor for merlin, the neurofibromatosis 2 tumor suppressor protein. NHE-RF mediates protein kinase A regulation of Na+-H+ exchanger NHE3 to which it is thought
to bind via one of its two PDZ domains. The carboxyl-terminal region of
NHE-RF, downstream of the PDZ domains, interacts with the
amino-terminal protein 4.1 domain-containing segment of merlin in yeast
two-hybrid assays. This interaction also occurs in affinity binding
assays with full-length NHE-RF expressed in COS-7 cells. NHE-RF binds
to the related ERM proteins, moesin and radixin. We have localized
human NHE-RF to actin-rich structures such as membrane ruffles,
microvilli, and filopodia in HeLa and COS-7 cells, where it
co-localizes with merlin and moesin. These findings suggest that
hNHE-RF and its binding partners may participate in a larger complex
(one component of which might be a Na+-H+
exchanger) that could be crucial for the actin filament assembly activated by the ERM proteins and for the tumor suppressor function of
merlin.
COMMUNICATION
NHE-RF, a Regulatory Cofactor for Na+-H+
Exchange, Is a Common Interactor for Merlin and ERM (MERM)
Proteins
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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