{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Koranne R"],"funding":["NIGMS NIH HHS"],"pagination":["113063"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12333389"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["413(2)"],"pubmed_abstract":["C9ORF78 is a poorly characterized protein found in diverse eukaryotes. Previous work indicated overexpression of C9ORF78 in malignant tissues indicating a possible involvement in growth regulatory pathways. Additional studies in fission yeast and humans uncover a potential function in regulating the spliceosome. In studies of GFP-tagged C9ORF78 we observed a dramatic reduction in protein abundance in cells grown to confluence and/or deprived of serum growth factors. Serum stimulation induced synchronous re-expression of the protein in HeLa cells. This effect was also observed with the endogenous protein. Overexpressing either E2F1 or N-Myc resulted in elevated C9ORF78 expression potentially explaining the serum-dependent upregulation of the protein. Immunofluorescence analysis indicates that C9ORF78 localizes to nuclei in interphase but does not appear to concentrate in speckles as would be expected for a splicing protein. Surprisingly, a subpopulation of C9ORF78 co-localizes with ACA, Mad1 and Ndc80 in mitotic cells suggesting that this protein associates with kinetochores or centromeres. Levels of C9ORF78 at the centromere/kinetochore also increased upon activation of the mitotic checkpoint. Furthermore, knocking-down C9ORF78 caused mitotic defects. These studies uncover novel mitotic function and subcellular localization of C9ORF78."],"journal":["Experimental cell research"],"pubmed_title":["C9ORF78 partially localizes to centromeres and plays a role in chromosome segregation."],"pmcid":["PMC12333389"],"funding_grant_id":["R15 GM141712","R15 GM120712"],"pubmed_authors":["Vandenbroek H","Brown K","Koranne R","Taylor WR"],"additional_accession":[]},"is_claimable":false,"name":"C9ORF78 partially localizes to centromeres and plays a role in chromosome segregation.","description":"C9ORF78 is a poorly characterized protein found in diverse eukaryotes. Previous work indicated overexpression of C9ORF78 in malignant tissues indicating a possible involvement in growth regulatory pathways. Additional studies in fission yeast and humans uncover a potential function in regulating the spliceosome. In studies of GFP-tagged C9ORF78 we observed a dramatic reduction in protein abundance in cells grown to confluence and/or deprived of serum growth factors. Serum stimulation induced synchronous re-expression of the protein in HeLa cells. This effect was also observed with the endogenous protein. Overexpressing either E2F1 or N-Myc resulted in elevated C9ORF78 expression potentially explaining the serum-dependent upregulation of the protein. Immunofluorescence analysis indicates that C9ORF78 localizes to nuclei in interphase but does not appear to concentrate in speckles as would be expected for a splicing protein. Surprisingly, a subpopulation of C9ORF78 co-localizes with ACA, Mad1 and Ndc80 in mitotic cells suggesting that this protein associates with kinetochores or centromeres. Levels of C9ORF78 at the centromere/kinetochore also increased upon activation of the mitotic checkpoint. Furthermore, knocking-down C9ORF78 caused mitotic defects. These studies uncover novel mitotic function and subcellular localization of C9ORF78.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2026-04-15T19:15:47.8Z","creation":"2026-04-07T14:00:54.762Z"},"accession":"S-EPMC12333389","cross_references":{"pubmed":["35167828"],"doi":["10.1016/j.yexcr.2022.113063"]}}