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Updated: Dec 31, 2025
Author Spotlight: Understanding Microtubule Network in Drosophila Neuromuscular Junctions
Published on: October 20, 2023
Drosophila Morgana is an Hsp90-interacting protein with a direct role in microtubule polymerisation
Valeria Palumbo1,2, Ammarah Tariq2, Lori Borgal2
1Dipartimento di Biologia e Biotecnologie Sapienza, Università di Roma, 00185 Rome, Italy valeria.palumbo@uniroma1.it j.g.wakefield@exeter.ac.uk.
Abstract:
Morgana (Mora, also known as CHORD in flies) and its mammalian homologue, called CHORDC1 or CHP1, is a highly conserved cysteine and histidine-rich domain (CHORD)-containing protein that has been proposed to function as an Hsp90 co-chaperone. Morgana deregulation promotes carcinogenesis in both mice and humans while, in Drosophila, loss of mora causes lethality and a complex mitotic phenotype that is rescued by a human morgana transgene. Here, we show that Drosophila Mora localises to mitotic spindles and co-purifies with the Hsp90-R2TP-TTT supercomplex and with additional well-known Hsp90 co-chaperones. Acute inhibition of Mora function in the early embryo results in a dramatic reduction in centrosomal microtubule stability, leading to small spindles nucleated from mitotic chromatin. Purified Mora binds to microtubules directly and promotes microtubule polymerisation in vitro, suggesting that Mora directly regulates spindle dynamics independently of its Hsp90 co-chaperone role.
Insights
Morgana (Mora) protein regulates microtubule stability during cell division. This study reveals its direct role in microtubule polymerization, independent of its Hsp90 co-chaperone function.
Area of Science:
- Cell Biology
- Molecular Biology
- Genetics
Background:
- Morgana (Mora) is a conserved CHORD-containing protein implicated in Hsp90 co-chaperoning.
- Morgana deregulation is linked to carcinogenesis, and its loss in Drosophila causes lethality and mitotic defects.
Purpose of the Study:
- To investigate the function of Drosophila Mora in mitosis.
- To determine if Mora's role in mitosis is linked to its Hsp90 co-chaperone activity.
Main Methods:
- Localization studies of Drosophila Mora in mitotic spindles.
- Co-purification with Hsp90-R2TP-TTT supercomplex and other Hsp90 co-chaperones.
- Functional inhibition of Mora in early embryos and in vitro microtubule polymerization assays.
Main Results:
- Drosophila Mora localizes to mitotic spindles and interacts with the Hsp90 machinery.
- Inhibition of Mora function leads to reduced microtubule stability and abnormal spindle formation.
- Purified Mora directly binds and promotes microtubule polymerization in vitro.
Conclusions:
- Drosophila Mora directly regulates microtubule dynamics and spindle organization.
- Mora's function in microtubule regulation is independent of its role as an Hsp90 co-chaperone.
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