Open AccessDrosophila Morgana is an Hsp90-interacting protein with a direct role in microtubule polymerization
Author(s) -
Valeria Palumbo,
Ammarah Tariq,
Lori Borgal,
Jeremy Metz,
Mara Brancaccio,
Maurizio Gatti,
James G. Wakefield,
Silvia Bonaccorsi
Publication year - 2020
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.236786
Subject(s) - biology , microbiology and biotechnology , mitosis , microtubule , chaperone (clinical) , medicine , pathology
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.