An interaction network of inner centriole proteins organised by POC1A-POC1B heterodimer crosslinks ensures centriolar integrity

Cornelia Sala, Martin Würtz, Enrico Salvatore Atorino, Annett Neuner, Patrick Partscht, Thomas Hoffmann, Sebastian Eustermann and Elmar Schiebel ()
Additional contact information
Cornelia Sala: Universität Heidelberg
Martin Würtz: Universität Heidelberg
Enrico Salvatore Atorino: European Molecular Biology Laboratory (EMBL) Heidelberg
Annett Neuner: Universität Heidelberg
Patrick Partscht: German Cancer Research Center (DKFZ)
Thomas Hoffmann: European Molecular Biology Laboratory (EMBL) Heidelberg
Sebastian Eustermann: European Molecular Biology Laboratory (EMBL) Heidelberg
Elmar Schiebel: Universität Heidelberg

Nature Communications, 2024, vol. 15, issue 1, 1-20

Abstract: Abstract Centriole integrity, vital for cilia formation and chromosome segregation, is crucial for human health. The inner scaffold within the centriole lumen composed of the proteins POC1B, POC5 and FAM161A is key to this integrity. Here, we provide an understanding of the function of inner scaffold proteins. We demonstrate the importance of an interaction network organised by POC1A-POC1B heterodimers within the centriole lumen, where the WD40 domain of POC1B localises close to the centriole wall, while the POC5-interacting WD40 of POC1A resides in the centriole lumen. The POC1A-POC5 interaction and POC5 tetramerization are essential for inner scaffold formation and centriole stability. The microtubule binding proteins FAM161A and MDM1 by binding to POC1A-POC1B, likely positioning the POC5 tetramer near the centriole wall. Disruption of POC1A or POC1B leads to centriole microtubule defects and deletion of both genes causes centriole disintegration. These findings provide insights into organisation and function of the inner scaffold.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-024-54247-5 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-54247-5

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-024-54247-5

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().