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Originally published In Press as doi:10.1074/jbc.M103013200 on September 4, 2001
J. Biol. Chem., Vol. 276, Issue 45, 42514-42519, November 9, 2001
Cytosolic Targeting Domains of and Calmodulin-dependent Protein Kinase II*
Nicole
Caran,
Lesley D.
Johnson,
Kimberley J.
Jenkins, and
Robert
M.
Tombes
From the Departments of Biology and Biochemistry and Molecular
Biophysics, Virginia Commonwealth University, Richmond Virginia
23284-2012
Ca2+/calmodulin-dependent
protein kinase II (CaMK-II) isozyme variability is the result of
alternative usage of variable domain sequences. Isozyme expression is
cell type-specific to transduce the appropriate Ca2+
signals. We have determined the subcellular targeting domain of
E CaMK-II, an isozyme that induces neurite outgrowth,
and of a structurally similar isozyme, C CaMK-II, which
does not induce neurite outgrowth. E CaMK-II
co-localizes with filamentous actin in the perinuclear region and in
cellular extensions. In contrast, C CaMK-II is uniformly
cytosolic. Constitutively active E CaMK-II induces
F-actin-rich extensions, thereby supporting a functional role for its
localization. C-terminal constructs, which lack central variable
domain sequences, can oligomerize and localize like full-length
E and C CaMK-II. Central variable domains
themselves are monomeric and have no targeting capability. The
C-terminal 95 residues of CaMK-II also has no targeting capability
but can efficiently oligomerize. These findings define a targeting
domain for and CaMK-IIs that is in between the central variable
and association domains. This domain is responsible for the subcellular
targeting differences between and CaMK-IIs.
*
This work was supported by grants from the Kate and Thomas
Jeffress Foundation Trust and the R. Clifton Brooks fund for Biomedical Research and by National Science Foundation Grant 9904765.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Depts. of
Biology and Biochemistry and Molecular Biophysics, Virginia
Commonwealth University, P. O. Box 842012, Richmond, VA
23284-2012. Tel.: 804-827-0141; Fax: 804-828-0503; E-mail:
rtombes@hsc.vcu.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.
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