| Literature DB >> 30659536 |
Claudio D'Amore1, Valentina Salizzato1,2, Christian Borgo1, Luca Cesaro1, Lorenzo A Pinna1,2, Mauro Salvi1.
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. Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.Keywords: Post-translational modifications; acidic phosphorylation; actin; casein kinase 2; septin; tubulin.
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Year: 2019 PMID: 30659536 DOI: 10.2174/1389203720666190119124846
Source DB: PubMed Journal: Curr Protein Pept Sci ISSN: 1389-2037 Impact factor: 3.272