Unknown

Dataset Information

0

The O-GlcNAc Transferase Intellectual Disability Mutation L254F Distorts the TPR Helix.


ABSTRACT: O-linked ?-N-acetyl-D-glucosamine (O-GlcNAc) transferase (OGT) regulates protein O-GlcNAcylation, an essential post-translational modification that is abundant in the brain. Recently, OGT mutations have been associated with intellectual disability, although it is not understood how they affect OGT structure and function. Using a multi-disciplinary approach we show that the L254F OGT mutation leads to conformational changes of the tetratricopeptide repeats and reduced activity, revealing the molecular mechanisms contributing to pathogenesis.

SUBMITTER: Gundogdu M 

PROVIDER: S-EPMC5967971 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

The O-GlcNAc Transferase Intellectual Disability Mutation L254F Distorts the TPR Helix.

Gundogdu Mehmet M   Llabrés Salomé S   Gorelik Andrii A   Ferenbach Andrew T AT   Zachariae Ulrich U   van Aalten Daan M F DMF  

Cell chemical biology 20180329 5


O-linked β-N-acetyl-<sub>D</sub>-glucosamine (O-GlcNAc) transferase (OGT) regulates protein O-GlcNAcylation, an essential post-translational modification that is abundant in the brain. Recently, OGT mutations have been associated with intellectual disability, although it is not understood how they affect OGT structure and function. Using a multi-disciplinary approach we show that the L254F OGT mutation leads to conformational changes of the tetratricopeptide repeats and reduced activity, reveali  ...[more]

Similar Datasets

| S-EPMC7253464 | biostudies-literature
| S-EPMC6660750 | biostudies-literature
2016-02-25 | E-GEOD-74263 | biostudies-arrayexpress
2016-02-25 | GSE74263 | GEO
| S-EPMC7042088 | biostudies-literature
| S-EPMC10309585 | biostudies-literature
| S-EPMC5493779 | biostudies-literature
| S-EPMC5535036 | biostudies-literature
2018-04-30 | GSE110616 | GEO
2018-02-26 | GSE107911 | GEO