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