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A Journey through the Cytoskeleton with Protein Kinase CK2

[ Vol. 20 , Issue. 6 ]

Author(s):

Claudio D'Amore, Valentina Salizzato, Christian Borgo, Luca Cesaro, Lorenzo A. Pinna and Mauro Salvi*   Pages 547 - 562 ( 16 )

Abstract:


Substrate pleiotropicity, a very acidic phosphorylation consensus sequence, and an apparent uncontrolled activity, are the main features of CK2, a Ser/Thr protein kinase that is required for a plethora of cell functions. Not surprisingly, CK2 appears to affect cytoskeletal structures and correlated functions such as cell shape, mechanical integrity, cell movement and division. This review outlines our current knowledge of how CK2 regulates cytoskeletal structures, and discusses involved pathways and molecular mechanisms.

Keywords:

Post-translational modifications, actin, tubulin, septin, casein kinase 2, acidic phosphorylation.

Affiliation:

Department of Biomedical Sciences, University of Padova, Via U. Bassi 58/B, Padova, Department of Biomedical Sciences, University of Padova, Via U. Bassi 58/B, Padova, Department of Biomedical Sciences, University of Padova, Via U. Bassi 58/B, Padova, Department of Biomedical Sciences, University of Padova, Via U. Bassi 58/B, Padova, Department of Biomedical Sciences, University of Padova, Via U. Bassi 58/B, Padova, Department of Biomedical Sciences, University of Padova, Via U. Bassi 58/B, Padova

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