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

4 Scopus citations


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)
Article numberbr14
JournalMolecular biology of the cell
Issue number9
StatePublished - Aug 1 2022

ASJC Scopus subject areas

  • General Medicine


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