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Aurora Kinase A proximity interactome reveals centriolar satellites as regulators of its function during primary cilium biogenesis

Melis D. Arslanhan, Navin Rauniyar, View ORCID ProfileJohn R. Yates III, View ORCID ProfileElif N. Firat-Karalar
doi: https://doi.org/10.1101/2020.11.05.370320
Melis D. Arslanhan
1Department of Molecular Biology and Genetics, Koç University, Istanbul, TURKEY 34450
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Navin Rauniyar
2Department of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
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John R. Yates III
2Department of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
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  • ORCID record for John R. Yates III
Elif N. Firat-Karalar
1Department of Molecular Biology and Genetics, Koç University, Istanbul, TURKEY 34450
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  • ORCID record for Elif N. Firat-Karalar
  • For correspondence: ekaralar@ku.edu.tr
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Abstract

Aurora kinase A (AURKA) is a conserved kinase that plays crucial roles in numerous cellular processes. Although AURKA overexpression is frequent in human cancers, its pleiotropic functions and complex spatiotemporal regulation have presented challenges in its therapeutic targeting. An essential step to overcome these challenges is the identification of the full range of AURKA regulators and substrates, which are often weak and transient. Previous proteomic studies were limited in monitoring dynamic and non-mitotic AURKA interactions. Here, we generated the first in vivo proximity interactome of AURKA, which consisted of over 100 proteins involving multiple biological processes and cellular compartments. Importantly, AURKA had extensive proximity interactions to centriolar satellites, key regulators of the primary cilium. Affinity pulldown and phosphoproteomics experiments confirmed this proximity relationship at the physical level. Loss-of-function experiments defined satellites as negative regulators of AURKA activity, abundance and localization in quiescent cells. Notably, loss of satellites increased AURKA activation at the basal body and resulted in defective cilium assembly and enhanced cilium disassembly. Collectively, our results provide a powerful resource for dissecting AURKA function and regulation and uncover proteostatic regulation of AURKA by centriolar satellites as a new regulatory mechanism for its non-mitotic functions.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted November 06, 2020.
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Aurora Kinase A proximity interactome reveals centriolar satellites as regulators of its function during primary cilium biogenesis
Melis D. Arslanhan, Navin Rauniyar, John R. Yates III, Elif N. Firat-Karalar
bioRxiv 2020.11.05.370320; doi: https://doi.org/10.1101/2020.11.05.370320
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Aurora Kinase A proximity interactome reveals centriolar satellites as regulators of its function during primary cilium biogenesis
Melis D. Arslanhan, Navin Rauniyar, John R. Yates III, Elif N. Firat-Karalar
bioRxiv 2020.11.05.370320; doi: https://doi.org/10.1101/2020.11.05.370320

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