Glucose binds and activates NSUN2 to promote translation and epidermal differentiation

Elevations in intracellular glucose concentrations are essential for epithelial cell differentiation by mechanisms that are not fully understood. Glucose has recently been found to directly bind several proteins to alter their functions to enhance differentiation. Among the newly identified glucose-binding proteins is NSUN2, an RNA-binding protein that we identified as indispensable for epidermal differentiation. Glucose was found to bind conserved sequences within NSUN2, enhancing its binding to S-adenosyl-L-methionine and boosting its enzymatic activity. Additionally, glucose enhanced NSUN2's proximity to proteins involved in mRNA translation, with NSUN2 modulating global messenger RNA (mRNA) translation, particularly that of key pro-differentiation mRNAs containing m5C modifications, such as GRHL3. Glucose thus engages diverse molecular mechanisms beyond its energetic roles to facilitate cellular differentiation processes.

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Publication Details

Journal
Nucleic Acids Research
Published
2024-11-20
DOI
https://doi.org/10.1093/nar/gkae1097
Citations
10
Primary Topic
RNA Research and Splicing
Type
article
Field-Weighted Citation Impact
2.34

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article

Glucose binds and activates NSUN2 to promote translation and epidermal differentiation

Shiying Tao, Paul A. Khavari, Yinsheng Wang, Vivian Tien et al.
10 citations
Nucleic Acids Research
RNA Research and Splicing
2.34
article

Glucose binds and activates NSUN2 to promote translation and epidermal differentiation

Shiying Tao, Paul A. Khavari, Yinsheng Wang, Vivian Tien, Paul B. Savage, Weili Miao, Ian Ferguson, Luca Ducoli, Vanessa Lopez-Pajares, Yen‐Yu Yang, Lindsey M. Meservey, Douglas F. Porter, Ya Li, Cheng-Jie Ma, Tom Jack
article en
10 citations

Abstract

Elevations in intracellular glucose concentrations are essential for epithelial cell differentiation by mechanisms that are not fully understood. Glucose has recently been found to directly bind several proteins to alter their functions to enhance differentiation. Among the newly identified glucose-binding proteins is NSUN2, an RNA-binding protein that we identified as indispensable for epidermal differentiation. Glucose was found to bind conserved sequences within NSUN2, enhancing its binding to S-adenosyl-L-methionine and boosting its enzymatic activity. Additionally, glucose enhanced NSUN2's proximity to proteins involved in mRNA translation, with NSUN2 modulating global messenger RNA (mRNA) translation, particularly that of key pro-differentiation mRNAs containing m5C modifications, such as GRHL3. Glucose thus engages diverse molecular mechanisms beyond its energetic roles to facilitate cellular differentiation processes.

Nucleic Acids ResearchVol. 52(22)
Brigham Young University (US), University of California, Riverside (US), VA Palo Alto Health Care System (US), Stanford University (US)
U.S. Department of Veterans Affairs, National Institutes of Health, National Institute of Arthritis and Musculoskeletal and Skin Diseases
Openalex Percentile: Top 11%
RNA Research and Splicing
2.34
DOIOpen Access PDFOpenAlex
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