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J Biol Chem, Vol. 274, Issue 3, 1621-1627, January 15, 1999
§,§
From the 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.
Ben May Institute for Cancer Research,
§ Department of Pharmacological and Physiological
Sciences, and ¶ Department of Pediatrics, University of
Chicago, Chicago, Illinois 60637
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