A point mutation in human coilin prevents Cajal body formation

0557827 - ÚMG 2023 RIV GB eng J - Journal Article
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
R&D Projects: GA MŠMT(CZ) LTAUSA18103; GA MŠMT(CZ) LM2015062; GA MŠMT(CZ) EF16_013/0001775; GA MŠMT LO1419
Institutional support: RVO:68378050
Keywords : Coilin * Cajal bodies * Mutation
OECD category: Cell biology
Impact factor: 4, year: 2022
Method of publishing: Limited access
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).
Permanent Link: http://hdl.handle.net/11104/0331723