Publication: Nuclear protein kinase C isoforms:
key players in multiple cell functions?
Authors
Martelli, A.M. ; Faenza, I. ; Billi, A.M. ; FalĂ , F. ; Cocco, L. ; Manzoli, L.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Protein kinase C (PKC) isozymes are a
family of serine/threonine protein kinases categorized
into three subfamilies: classical, novel, and atypical.
PKC isozymes, whose expression is cell type-specific
and developmentally regulated, are key transducers in
many agonist-induced signaling cascades. To date at
least 10 different PKC isotypes have been identified and
are believed to play distinct regulatory roles. PKC
isoforms are catalytically activated by several lipid
cofactors, including diacylglycerol. PKC is thought to
reside in the cytoplasm in an inactive conformation and
to translocate to the plasma membrane or cytoplasmic
organelles upon cell activation by different stimuli.
However, a sizable body of evidence collected over the
last 15 years has shown PKC to be capable of
translocating to the nucleus. Furthermore, PKC isoforms
can reside within the nucleus. Studies from independent
laboratories have to led to the identification of several
nuclear proteins which act as PKC substrates as well as
to the characterization of some nuclear PKC-binding
proteins which may be of fundamental importance for
finely tuning PKC function in this peculiar cell
microenvironment. Most likely, nuclear PKC isozymes
are involved in the regulation of several important
biological processes such as cell proliferation and
differentiation, neoplastic transformation, and apoptosis.
In this review, we shall summarize the most intriguing
evidence about the roles played by nuclear PKC
isozymes.
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