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J Biol Chem, Vol. 274, Issue 3, 1621-1627, January 15, 1999

Molecular Cloning and Characterization of a Mitogen-activated Protein Kinase-associated Intracellular Chloride Channel

Zhijian Qian^§, Dayne Okuhara^§, Mark K. Abe^¶, and Marsha Rich Rosner^§

From the  Ben May Institute for Cancer Research, ^§ Department of Pharmacological and Physiological Sciences, and ^¶ Department of Pediatrics, University of Chicago, Chicago, Illinois 60637

ERK7, a member of the mitogen-activated protein kinase family, has a carboxyl-terminal tail that is required for ERK7 activation, cellular localization, and its ability to inhibit DNA synthesis. To identify proteins that interact with ERK7, we utilized a yeast two-hybrid screen with the COOH-terminal tail of ERK7 as bait and isolated the cDNA for a novel protein termed CLIC3. The interaction between CLIC3 and ERK7 in mammalian cells was confirmed by co-immunoprecipitation. CLIC3 has significant homology to human intracellular chloride channels 1 (NCC27/CLIC1) and 2 and bovine kidney chloride channel p64. Like NCC27/CLIC1, CLIC3 is predominantly localized in the nucleus and stimulates chloride conductance when expressed in cells. Taken together, these results suggest that CLIC3 is a new member of the human CLIC family. The observed interaction between CLIC3 and ERK7 is the first demonstration of a stable complex between a protein that activates chloride ion transport and a member of the mitogen-activated protein kinase family of signal transducers. The specific association of CLIC3 with the COOH-terminal tail of ERK7 suggests that CLIC3 may play a role in the regulation of cell growth.

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