<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Palumbo V</submitter><funding>Associazione Italiana per la Ricerca sul Cancro</funding><funding>Royal Society</funding><funding>Biotechnology and Biological Sciences Research Council</funding><pagination>jcs236786</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6983718</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>133(2)</volume><pubmed_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. Puri</pubmed_abstract><journal>Journal of cell science</journal><pubmed_title>Drosophila Morgana is an Hsp90-interacting protein with a direct role in microtubule polymerisation.</pubmed_title><pmcid>PMC6983718</pmcid><funding_grant_id>NF151014</funding_grant_id><funding_grant_id>BB/K017837/1</funding_grant_id><funding_grant_id>IG 20528</funding_grant_id><funding_grant_id>BB/K017937/1</funding_grant_id><pubmed_authors>Metz J</pubmed_authors><pubmed_authors>Gatti M</pubmed_authors><pubmed_authors>Tariq A</pubmed_authors><pubmed_authors>Brancaccio M</pubmed_authors><pubmed_authors>Bonaccorsi S</pubmed_authors><pubmed_authors>Borgal L</pubmed_authors><pubmed_authors>Palumbo V</pubmed_authors><pubmed_authors>Wakefield JG</pubmed_authors></additional><is_claimable>false</is_claimable><name>Drosophila Morgana is an Hsp90-interacting protein with a direct role in microtubule polymerisation.</name><description>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. Puri</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Jan</publication><modification>2025-04-18T15:51:37.142Z</modification><creation>2020-05-22T08:34:29Z</creation></dates><accession>S-EPMC6983718</accession><cross_references><pubmed>31907206</pubmed><doi>10.1242/jcs.236786</doi></cross_references></HashMap>