A point mutation in human coilin prevents Cajal body formation

0557827 - ÚMG 2023 RIV GB eng J - Článek v odborném periodiku
Basello, Davide Allesandro - Matera, A. - Staněk, David
A point mutation in human coilin prevents Cajal body formation.
Journal of Cell Science. Roč. 135, č. 8 (2022), č. článku jcs259587. ISSN 0021-9533. E-ISSN 1477-9137
Grant CEP: GA MŠMT(CZ) LTAUSA18103; GA MŠMT(CZ) LM2015062; GA MŠMT(CZ) EF16_013/0001775; GA MŠMT LO1419
Institucionální podpora: RVO:68378050
Klíčová slova: Coilin * Cajal bodies * Mutation
Obor OECD: Cell biology
Impakt faktor: 4, rok: 2022
Způsob publikování: Omezený přístup
https://journals.biologists.com/jcs/article-abstract/135/8/jcs259587/275105/A-point-mutation-in-human-coilin-prevents-Cajal?redirectedFrom=fulltext

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 interpreting data from coilin plasmids that are derived from this variant (currently deposited at Addgene).
Trvalý link: http://hdl.handle.net/11104/0331723