RT Journal Article
SR Electronic
T1 FAM83D directs protein kinase CK1α to the mitotic spindle for proper spindle positioning
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 480616
DO 10.1101/480616
A1 Luke J. Fulcher
A1 Zhengcheng He
A1 Lin Mei
A1 Thomas J. Macartney
A1 Nicola T. Wood
A1 Alan R. Prescott
A1 Arlene J. Whigham
A1 Joby Varghese
A1 Robert Gourlay
A1 Graeme Ball
A1 Rosemary Clarke
A1 David G. Campbell
A1 Christopher A. Maxwell
A1 Gopal P. Sapkota
YR 2018
UL http://biorxiv.org/content/early/2018/11/27/480616.abstract
AB 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 FAM83DF283A/F283A knockin mutation, 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 FAM83DF283A/F283A cells, rescues these defects. These findings implicate CK1α as new mitotic kinase that orchestrates the kinetics and orientation of cell division.