Patronin condensation integrates recognition, protection and organization of microtubule minus ends
- 1MOE Key Laboratory of Model Animals for Disease Study, Department of Laboratory Medicine, Nanjing Drum Tower Hospital, The Affiliated Hospital of Nanjing Univer
Abstract
Microtubule minus ends are central to non-centrosomal microtubule organization, yet how their recognition, protection and molecular organization are integrated remains unclear. Here we show that Drosophila Patronin forms dynamic condensates at microtubule minus ends through a prion-like domain (PrLD). PrLD-mediated condensation cooperates with the CKK domain and a second CKK-independent recognition region to convert weak or broadly distributed microtubule-binding activities into persistent minus-end recognition and tracking. Replacing the PrLD with a heterologous phase-separating HNRNPA1 IDR restores minus-end targeting, indicating that condensation capacity rather than PrLD primary sequence is critical. Patronin condensates further form a protective cap that resists minus-end depolymerization and recruit the cytoskeletal regulators Sas-4, Katanin and Ena. Disrupting PrLD multivalency impairs Patronin localization at multiple developmental sites and causes early organismal lethality. Thus, Patronin condensation creates a physiologically essential microtubule minus-end compartment coupling end recognition, stabilization and cytoskeletal organization.
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BibTeX
@misc{zhang2026patronin,
title = {{Patronin condensation integrates recognition, protection and organization of microtubule minus ends}},
author = {B. Zhang and J. Yang and S. Yu and K. Zhou and L. He and L. Huang and X. Liang and H. Wang and J. Chen},
howpublished = {bioRxiv},
year = {2026},
month = oct,
doi = {10.64898/2026.10.03.756418},
url = {https://www.biorxiv.org/content/10.64898/2026.10.03.756418v1},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - Patronin condensation integrates recognition, protection and organization of microtubule minus ends
AU - B. Zhang
AU - J. Yang
AU - S. Yu
AU - K. Zhou
AU - L. He
AU - L. Huang
AU - X. Liang
AU - H. Wang
AU - J. Chen
PY - 2026
DA - 2026/10/03
PB - bioRxiv
DO - 10.64898/2026.10.03.756418
UR - https://www.biorxiv.org/content/10.64898/2026.10.03.756418v1
AB - Microtubule minus ends are central to non-centrosomal microtubule organization, yet how their recognition, protection and molecular organization are integrated remains unclear. Here we show that Drosophila Patronin forms dynamic condensates at microtubule minus ends through a prion-like domain (PrLD). PrLD-mediated condensation cooperates with the CKK domain and a second CKK-independent recognition region to convert weak or broadly distributed microtubule-binding activities into persistent minus-end recognition and tracking. Replacing the PrLD with a heterologous phase-separating HNRNPA1 IDR restores minus-end targeting, indicating that condensation capacity rather than PrLD primary sequence is critical. Patronin condensates further form a protective cap that resists minus-end depolymerization and recruit the cytoskeletal regulators Sas-4, Katanin and Ena. Disrupting PrLD multivalency impairs Patronin localization at multiple developmental sites and causes early organismal lethality. Thus, Patronin condensation creates a physiologically essential microtubule minus-end compartment coupling end recognition, stabilization and cytoskeletal organization.
ER -