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Journal of Neuroscience, Vol 15, 6797-6808, Copyright © 1995 by Society for Neuroscience
Developmental and regional expression of multifunctional Ca2+/calmodulin-dependent protein kinase isoforms in rat brain
L Brocke, M Srinivasan and H Schulman
Department of Neurobiology, Stanford University School of Medicine, California 94305-5401, USA.
Multifunctional Ca2+/calmodulin-dependent protein kinase (CaM kinase)
participates in diverse calcium signaling pathways in neurons. The alpha-
and beta-CaM kinase isoforms are neuron-specific and highly abundant in rat
brain. The variable domain of CaM kinase is a potential site for the
generation of isoform diversity by alternative spicing of its N- and/or
C-terminal segments. We used specific PCR primers which span the variable
domain of either alpha- or beta-CaM kinase and isolated three new isoforms
from rat brain, namely alpha B-, beta e- and beta'e-CaM kinase. alpha
beta-CaM kinase contains 11 amino acids, likely inserted by alternative
splicing, at the C-terminal segment of the variable domain. This insertion
introduces a nuclear localization signal (NLS) that targets alpha B-CaM
kinase to the nucleus of transfected cells; alpha-CaM kinase is excluded
from the nucleus. The mRNA and the protein corresponding to this isoform
are detected only in the diencephalon/midbrain regions. We have also
identified two alternatively spliced isoforms of beta-CaM kinase that lack
the 24 amino acid sequence at the N-terminal segment of the variable
domain. Alternative splicing of these two isoforms occurs with a three base
pair shift of the 3'-splice site. Our analysis shows that these new
beta-CaM kinase isoforms are expressed primarily in early developmental
stages, and we therefore term them beta e - (embryonic) and beta' e-CaM
kinase. Recombinant alpha B-, beta e and beta' e-CaM kinase expressed in
COS-7 cells exhibit characteristic Ca2+/calmodulin-dependent protein kinase
activity and autophosphorylation.
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