Protein Kinase C, Focal Adhesions and the Regulation of Cell Migration

被引:61
作者
Fogh, Betina S. [1 ]
Multhaupt, Hinke A. B. [1 ]
Couchman, John R. [1 ]
机构
[1] Univ Copenhagen, Dept Biomed Sci, DK-2200 Copenhagen N, Denmark
基金
新加坡国家研究基金会;
关键词
Kinase; Microfilaments; Proteoglycan; Cytoskeleton; Adhesion; PHOSPHOINOSITIDE-DEPENDENT KINASE; PKC-ALPHA; TYROSINE PHOSPHORYLATION; CYTOPLASMIC DOMAIN; CATALYTIC DOMAIN; MATRIX ADHESIONS; MEDIATED PHOSPHORYLATION; ALPHA(5)BETA(1) INTEGRIN; RAC1; ACTIVATION; STRESS FIBERS;
D O I
10.1369/0022155413517701
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Cell adhesion to extracellular matrix is a complex process involving protrusive activity driven by the actin cytoskeleton, engagement of specific receptors, followed by signaling and cytoskeletal organization. Thereafter, contractile and endocytic/recycling activities may facilitate migration and adhesion turnover. Focal adhesions, or focal contacts, are widespread organelles at the cell-matrix interface. They arise as a result of receptor interactions with matrix ligands, together with clustering. Recent analysis shows that focal adhesions contain a very large number of protein components in their intracellular compartment. Among these are tyrosine kinases, which have received a great deal of attention, whereas the serine/threonine kinase protein kinase C has received much less. Here the status of protein kinase C in focal adhesions and cell migration is reviewed, together with discussion of its roles and potential substrates.
引用
收藏
页码:172 / 184
页数:13
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