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FAM 83D directs protein kinase CK 1α to the mitotic spindle for proper spindle positioning
Author(s) -
Fulcher Luke J,
He Zhengcheng,
Mei Lin,
Macartney Thomas J,
Wood Nicola T,
Prescott Alan R,
Whigham Arlene J,
Varghese Joby,
Gourlay Robert,
Ball Graeme,
Clarke Rosemary,
Campbell David G,
Maxwell Christopher A,
Sapkota Gopal P
Publication year - 2019
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201847495
Subject(s) - microbiology and biotechnology , casein kinase 1 , mitosis , polo like kinase , mitotic exit , spindle apparatus , biology , spindle checkpoint , kinase , spindle pole body , cell division , protein kinase a , cell cycle , cell , biochemistry
The concerted action of many protein kinases helps orchestrate the error‐free progression through mitosis of mammalian cells. The roles and regulation of some prominent mitotic kinases, such as cyclin‐dependent kinases, are well established. However, these and other known mitotic kinases alone cannot account for the extent of protein phosphorylation that has been reported during mammalian mitosis. Here we demonstrate that CK1α, of the casein kinase 1 family of protein kinases, localises to the spindle and is required for proper spindle positioning and timely cell division. CK1α is recruited to the spindle by FAM83D, and cells devoid of FAM83D , or those harbouring CK1α‐binding‐deficient FAM83D F283A/F283A knockin mutations, display pronounced spindle positioning defects, and a prolonged mitosis. Restoring FAM83D at the endogenous locus in FAM83D − / − cells, or artificially delivering CK1α to the spindle in FAM83D F283A/F283A cells, rescues these defects. These findings implicate CK1α as new mitotic kinase that orchestrates the kinetics and orientation of cell division.