TY - JOUR
T1 - Pericentriolar matrix (PCM) integrity relies on cenexin and polo-like kinase (PLK)1
AU - Aljiboury, Abrar
AU - Mujcic, Amra
AU - Curtis, Erin
AU - Cammerino, Thomas
AU - Magny, Denise
AU - Lan, Yiling
AU - Bates, Michael
AU - Freshour, Judy
AU - Ahmed-Braimeh, Yasir H.
AU - Hehnly, Heidi
N1 - Publisher Copyright:
© 2022 Aljiboury et al.
PY - 2022/8/1
Y1 - 2022/8/1
N2 - Polo-like-kinase (PLK) 1 activity is associated with maintaining the functional and physical properties of the centrosome’s pericentriolar matrix (PCM). In this study, we use a multimodal approach of human cells (HeLa), zebrafish embryos, and phylogenic analysis to test the role of a PLK1 binding protein, cenexin, in regulating the PCM. Our studies identify that cenexin is required for tempering microtubule nucleation by maintaining PCM cohesion in a PLK1-dependent manner. PCM architecture in cenexin-depleted zebrafish embryos was rescued with wild-type human cenexin, but not with a C-terminal cenexin mutant (S796A) deficient in PLK1 binding. We propose a model where cenexin’s C terminus acts in a conserved manner in eukaryotes, excluding nematodes and arthropods, to sequester PLK1 that limits PCM substrate phosphorylation events required for PCM cohesion.
AB - Polo-like-kinase (PLK) 1 activity is associated with maintaining the functional and physical properties of the centrosome’s pericentriolar matrix (PCM). In this study, we use a multimodal approach of human cells (HeLa), zebrafish embryos, and phylogenic analysis to test the role of a PLK1 binding protein, cenexin, in regulating the PCM. Our studies identify that cenexin is required for tempering microtubule nucleation by maintaining PCM cohesion in a PLK1-dependent manner. PCM architecture in cenexin-depleted zebrafish embryos was rescued with wild-type human cenexin, but not with a C-terminal cenexin mutant (S796A) deficient in PLK1 binding. We propose a model where cenexin’s C terminus acts in a conserved manner in eukaryotes, excluding nematodes and arthropods, to sequester PLK1 that limits PCM substrate phosphorylation events required for PCM cohesion.
UR - http://www.scopus.com/inward/record.url?scp=85134854932&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85134854932&partnerID=8YFLogxK
U2 - 10.1091/mbc.E22-01-0015
DO - 10.1091/mbc.E22-01-0015
M3 - Article
C2 - 35609215
AN - SCOPUS:85134854932
SN - 1059-1524
VL - 33
JO - Molecular biology of the cell
JF - Molecular biology of the cell
IS - 9
M1 - br14
ER -