4.3 Review

A Journey through the Cytoskeleton with Protein Kinase CK2

期刊

CURRENT PROTEIN & PEPTIDE SCIENCE
卷 20, 期 6, 页码 547-562

出版社

BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/1389203720666190119124846

关键词

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

资金

  1. Fondazione per la Ricerca sulla Fibrosi Cistica (grant FFC) [10/2016, 12/2017]
  2. University of Padova [BIRD173809/17]
  3. Associazione Italiana per la Ricerca sul Cancro (AIRC) [IG 18756]

向作者/读者索取更多资源

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.

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