PCMD-1 stabilizes the PCM scaffold and facilitates centriole separation
Schreiner A, Heim A, Pletschacher L, Alznauer LM, Schwenkert S, Friederike W, Zanin E, Mikeladze-Dvali T (2025)
Publication Type: Journal article
Publication year: 2025
Journal
Book Volume: 224
Article Number: e202411107
Issue: 12
Abstract
Centrosomes are highly dynamic organelles, and maintaining their stability is crucial for spindle pole integrity and bipolar spindle formation. Centrosomes consist of a pair of centrioles surrounded by the PCM. In Caenorhabditis elegans, interactions between the scaffold protein SPD-5 and kinase PLK-1 are essential for PCM formation. However, how PCM stability is established and maintained remains unclear. We address this by analyzing the function of PCMD-1, a protein mainly localizing to centrioles. We show that CDK-1 primes PCMD-1 for PLK-1 phosphorylation. Mutations in PLK-1 docking sites abolish PCMD-1 phosphorylation and SPD-5 binding in vitro and destabilize the PCM scaffold in vivo. As a result, microtubule-pulling forces cannot be relayed to centrioles, delaying their separation. Our findings reveal that PCMD-1 is critical for PCM stability and timely centriole separation during PCM disassembly. We propose that PCMD-1 initiates scaffold assembly by biasing the PCM core toward intrinsic order, acting as a seed that propagates throughout the scaffold to ensure structural integrity.
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Germany (DE)How to cite
APA:
Schreiner, A., Heim, A., Pletschacher, L., Alznauer, L.-M., Schwenkert, S., Friederike, W.,... Mikeladze-Dvali, T. (2025). PCMD-1 stabilizes the PCM scaffold and facilitates centriole separation. The Journal of Cell Biology, 224. https://doi.org/10.1083/jcb.202411107
MLA:
Schreiner, Alina, et al. "PCMD-1 stabilizes the PCM scaffold and facilitates centriole separation." The Journal of Cell Biology 224 (2025).
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