Drosophila Morgana is an Hsp90-interacting protein with a direct role in microtubule polymerisation.
J Cell Sci
; 133(2)2020 01 23.
Article
in En
| MEDLINE
| ID: mdl-31907206
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
HSP90 Heat-Shock Proteins
/
Drosophila Proteins
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Microtubules
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Mitosis
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Spindle Apparatus
Limits:
Animals
/
Humans
Language:
En
Journal:
J Cell Sci
Year:
2020
Document type:
Article