A Structural Study of the Cytoplasmic Chaperone Effect of 14-3-3 Proteins on Ataxin-1

[Display omitted] •14-3-3 was postulated to prevent cytoplasmic aggregation of Ataxin-1.•Experimental support for an anti-aggregation effect of 14-3-3 on Ataxin-1 is provided.•Structural studies suggest 14-3-3 reduces Ataxin-1 dimerisation and further self-association.•Modulation of the 14-3-3/Ataxi...

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Bibliographic Details
Published in:	Journal of molecular biology Vol. 433; no. 19; p. 167174
Main Authors:	Leysen, Seppe, Burnley, Rebecca Jane, Rodriguez, Elizabeth, Milroy, Lech-Gustav, Soini, Lorenzo, Adamski, Carolyn J., Nitschke, Larissa, Davis, Rachel, Obsil, Tomas, Brunsveld, Lucas, Crabbe, Tom, Zoghbi, Huda Yahya, Ottmann, Christian, Davis, Jeremy Martin
Format:	Journal Article
Language:	English
Published:	Netherlands Elsevier Ltd 17.09.2021 Elsevier
Subjects:	14-3-3 Proteins - metabolism Ataxin-1 - chemistry Ataxin-1 - metabolism Binding Sites Cell Line crystal structure Crystallography, X-Ray Cytoplasm - metabolism dimerization HDX-MS HEK293 Cells Humans molecular biology mutants neurodegeneration neurodegenerative diseases Phosphorylation protein aggregation Protein Domains Protein Multimerization Protein Stability SAXS serine pS SUMO DSS SCA1 neurodegeneration AXH domain SAXS HDX-MS NLS protein aggregation crystal structure DSG ITC polyQ CIC
ISSN:	0022-2836, 1089-8638, 1089-8638
Online Access:	Get full text
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