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Protein kinase C and the regulation of the actin cytoskeleton.

Larsson, Christer LU (2006) In Cellular Signalling 18(3). p.276-284
Abstract
Protein kinase C (PKC) isoforms are central components in intracellular networks that regulate a vast number of cellular processes. It has long been known that in most cell types, one or more PKC isoforms influences the morphology of the F-actin cytoskeleton and thereby regulates processes that are affected by remodelling of the microfilaments. These include cellular migration and neurite outgrowth. This review focuses on the role of classical and novel PKC isoforms in migration and neurite outgrowth, and highlights some regulatory steps that may be of importance in the regulation by PKC of migration and neurite outgrowth. Many studies indicate that integrins are crucial mediators both upstream and downstream of PKC in inducing... (More)
Protein kinase C (PKC) isoforms are central components in intracellular networks that regulate a vast number of cellular processes. It has long been known that in most cell types, one or more PKC isoforms influences the morphology of the F-actin cytoskeleton and thereby regulates processes that are affected by remodelling of the microfilaments. These include cellular migration and neurite outgrowth. This review focuses on the role of classical and novel PKC isoforms in migration and neurite outgrowth, and highlights some regulatory steps that may be of importance in the regulation by PKC of migration and neurite outgrowth. Many studies indicate that integrins are crucial mediators both upstream and downstream of PKC in inducing morphological changes. Furthermore, a number of PKC substrates, directly associated with the microfilaments, such as MARCKS, GAP43, adducin, fascin, ERM proteins and others have been identified. Their potential role in PKC effects on the cytoskeleton is discussed. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
fibers, integrins, cell movement, neurite, stress, protein kinase C, actin
in
Cellular Signalling
volume
18
issue
3
pages
276 - 284
publisher
Elsevier
external identifiers
  • wos:000233954800002
  • pmid:16109477
  • scopus:27844539756
  • pmid:16109477
ISSN
1873-3913
DOI
10.1016/j.cellsig.2005.07.010
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Tumour Cell Biology (013017530)
id
1d2a27c5-5532-4672-a5a1-f0482f5c5f22 (old id 142663)
date added to LUP
2016-04-01 12:02:05
date last changed
2022-04-28 23:34:12
@article{1d2a27c5-5532-4672-a5a1-f0482f5c5f22,
  abstract     = {{Protein kinase C (PKC) isoforms are central components in intracellular networks that regulate a vast number of cellular processes. It has long been known that in most cell types, one or more PKC isoforms influences the morphology of the F-actin cytoskeleton and thereby regulates processes that are affected by remodelling of the microfilaments. These include cellular migration and neurite outgrowth. This review focuses on the role of classical and novel PKC isoforms in migration and neurite outgrowth, and highlights some regulatory steps that may be of importance in the regulation by PKC of migration and neurite outgrowth. Many studies indicate that integrins are crucial mediators both upstream and downstream of PKC in inducing morphological changes. Furthermore, a number of PKC substrates, directly associated with the microfilaments, such as MARCKS, GAP43, adducin, fascin, ERM proteins and others have been identified. Their potential role in PKC effects on the cytoskeleton is discussed.}},
  author       = {{Larsson, Christer}},
  issn         = {{1873-3913}},
  keywords     = {{fibers; integrins; cell movement; neurite; stress; protein kinase C; actin}},
  language     = {{eng}},
  number       = {{3}},
  pages        = {{276--284}},
  publisher    = {{Elsevier}},
  series       = {{Cellular Signalling}},
  title        = {{Protein kinase C and the regulation of the actin cytoskeleton.}},
  url          = {{http://dx.doi.org/10.1016/j.cellsig.2005.07.010}},
  doi          = {{10.1016/j.cellsig.2005.07.010}},
  volume       = {{18}},
  year         = {{2006}},
}