2021
DOI: 10.1007/s00018-021-03992-7
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Nuclear import receptors and hnRNPK mediates nuclear import and stress granule localization of SIRLOIN

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Cited by 3 publications
(2 citation statements)
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“…The third KH domain of hnRNP-K KH3 has been shown to bind to nucleic acids as an isolated domain, although, exhibiting lower affinity than the full-length protein ( 98 ). These previous studies have observed that the KH3 domains bind to TCCC or CCCC-rich as well as CCTC C/T-rich motifs ( 98 , 99 ). Two TCCC motifs are present in the sense LincRNA-p21 AluSx1 RNA in both the 5′-junction and 3′-three-way junctions.…”
Section: Discussionmentioning
confidence: 82%
“…The third KH domain of hnRNP-K KH3 has been shown to bind to nucleic acids as an isolated domain, although, exhibiting lower affinity than the full-length protein ( 98 ). These previous studies have observed that the KH3 domains bind to TCCC or CCCC-rich as well as CCTC C/T-rich motifs ( 98 , 99 ). Two TCCC motifs are present in the sense LincRNA-p21 AluSx1 RNA in both the 5′-junction and 3′-three-way junctions.…”
Section: Discussionmentioning
confidence: 82%
“…The structure of the KH domain of hnRNPK in association with ssDNA has been solved by X-ray crystallography (hnRNPK PDB: 7CRE). It was demonstrated to associate with RNA via multiple weak interactions ( Yao et al, 2021 ). Mutations in both copies of hnRNPK in diploid cells are embryonic lethal in mice ( Gallardo et al, 2015 ), whereas mutation of a single copy causes Au–Kline syndrome characterized by hypotonia, learning disability, and delayed development ( Au et al, 1993 ).…”
Section: Membrane Associations Of Kh Domain Proteinsmentioning
confidence: 99%