Pericentriolar matrix (PCM) integrity relies on cenexin and polo-like kinase (PLK)1

Abrar Aljiboury, Amra Mujcic, Erin Curtis, Thomas Cammerino, Denise Magny, Yiling Lan, Michael Bates, Judy Freshour, Yasir H. Ahmed-Braimeh, Heidi Hehnly

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Pages (from-to)br14
JournalMolecular biology of the cell
Issue number9
StatePublished - Aug 1 2022

ASJC Scopus subject areas

  • Medicine(all)


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