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
- Fondazione per la Ricerca sulla Fibrosi Cistica (grant FFC) [10/2016, 12/2017]
- University of Padova [BIRD173809/17]
- Associazione Italiana per la Ricerca sul Cancro (AIRC) [IG 18756]
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据