{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Basello DA"],"funding":["Grantov Agentura, Univerzita Karlova","Akademie Věd České Republiky","Ministerstvo","Akademie Vʃd ɨesk Republiky","Ministerstvo Školství, Mládeže a Tělovýchovy","National Institutes of Health","Grantová Agentura, Univerzita Karlova","NIGMS NIH HHS"],"pagination":["jcs259587"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9080554"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["135(8)"],"pubmed_abstract":["Coilin is a conserved protein essential for integrity of nuclear membrane-less inclusions called Cajal bodies. Here, we report an amino acid substitution (p.K496E) found in a widely-used human EGFP-coilin construct that has a dominant-negative effect on Cajal body formation. We show that this coilin-K496E variant fails to rescue Cajal bodies in cells lacking endogenous coilin, whereas the wild-type construct restores Cajal bodies in mouse and human coilin-knockout cells. In cells containing endogenous coilin, both the wild-type and K496E variant proteins accumulate in Cajal bodies. However, high-level overexpression of coilin-K496E causes Cajal body disintegration. Thus, a mutation in the C-terminal region of human coilin can disrupt Cajal body assembly. Caution should be used when interpr"],"journal":["Journal of cell science"],"pubmed_title":["A point mutation in human coilin prevents Cajal body formation."],"pmcid":["PMC9080554"],"funding_grant_id":["1650218","RVO68378050-KAV-NPUI","RVO68378050","R35 GM136435","R35-GM136435","LTAUSA18103"],"pubmed_authors":["Stanek D","Matera AG","Basello DA"],"additional_accession":[]},"is_claimable":false,"name":"A point mutation in human coilin prevents Cajal body formation.","description":"Coilin is a conserved protein essential for integrity of nuclear membrane-less inclusions called Cajal bodies. Here, we report an amino acid substitution (p.K496E) found in a widely-used human EGFP-coilin construct that has a dominant-negative effect on Cajal body formation. We show that this coilin-K496E variant fails to rescue Cajal bodies in cells lacking endogenous coilin, whereas the wild-type construct restores Cajal bodies in mouse and human coilin-knockout cells. In cells containing endogenous coilin, both the wild-type and K496E variant proteins accumulate in Cajal bodies. However, high-level overexpression of coilin-K496E causes Cajal body disintegration. Thus, a mutation in the C-terminal region of human coilin can disrupt Cajal body assembly. Caution should be used when interpr","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2026-05-09T19:47:05.461Z","creation":"2025-02-19T04:16:13.296Z"},"accession":"S-EPMC9080554","cross_references":{"pubmed":["35356988"],"doi":["10.1242/jcs.259587"]}}