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Title: Novel nucleocytoplasmic protein O-fucosylation by SPINDLY regulates diverse developmental processes in plants

Abstract

Here, in metazoans, protein O-fucosylation of Ser/Thr residues was only found in secreted or cell surface proteins, and this post-translational modification is catalyzed by ER-localized protein O-fucosyltransferases (POFUTs) in the GT65 family. Recently, a novel nucleocytoplasmic POFUT, SPINDLY (SPY), was identified in the reference plant Arabidopsis thaliana to modify nuclear transcription regulators DELLAs, revealing a new regulatory mechanism for gene expression. The paralog of AtSPY, SECRET AGENT (SEC), is an O-link-N-acetylglucosamine (GlcNAc) transferase (OGT), which O-GlcNAcylates Ser/Thr residues of target proteins. Both AtSPY and AtSEC are tetratricopeptide repeat-domain-containing glycosyltransferases in the GT41 family. The discovery that AtSPY is a POFUT clarified decades of miss-classification of AtSPY as an OGT. SPY and SEC play pleiotropic roles in plant development, and the interactions between SPY and SEC are complex. SPY-like genes are conserved in diverse organisms, except in fungi and metazoans, suggesting that O-fucosylation is a common mechanism in modulating intracellular protein functions.

Authors:
 [1]
  1. Duke Univ., Durham, NC (United States)
Publication Date:
Research Org.:
Duke Univ., Durham, NC (United States)
Sponsoring Org.:
USDOE Office of Science (SC); National Institutes of Health (NIH); National Science Foundation (NSF); USDA
OSTI Identifier:
1853182
Alternate Identifier(s):
OSTI ID: 1778488
Grant/Contract Number:  
SC0019393; 2R01 GM100051-05A1; MCB-1818161; 2018-67013-27395
Resource Type:
Accepted Manuscript
Journal Name:
Current Opinion in Structural Biology
Additional Journal Information:
Journal Volume: 68; Journal Issue: C; Journal ID: ISSN 0959-440X
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; protein O-fucosylation; protein O-GlcNAcylation; nucleocytoplasmic protein O-fucosylation; SPINDLY; POFUT

Citation Formats

Sun, Tai-ping. Novel nucleocytoplasmic protein O-fucosylation by SPINDLY regulates diverse developmental processes in plants. United States: N. p., 2021. Web. doi:10.1016/j.sbi.2020.12.013.
Sun, Tai-ping. Novel nucleocytoplasmic protein O-fucosylation by SPINDLY regulates diverse developmental processes in plants. United States. https://doi.org/10.1016/j.sbi.2020.12.013
Sun, Tai-ping. Mon . "Novel nucleocytoplasmic protein O-fucosylation by SPINDLY regulates diverse developmental processes in plants". United States. https://doi.org/10.1016/j.sbi.2020.12.013. https://www.osti.gov/servlets/purl/1853182.
@article{osti_1853182,
title = {Novel nucleocytoplasmic protein O-fucosylation by SPINDLY regulates diverse developmental processes in plants},
author = {Sun, Tai-ping},
abstractNote = {Here, in metazoans, protein O-fucosylation of Ser/Thr residues was only found in secreted or cell surface proteins, and this post-translational modification is catalyzed by ER-localized protein O-fucosyltransferases (POFUTs) in the GT65 family. Recently, a novel nucleocytoplasmic POFUT, SPINDLY (SPY), was identified in the reference plant Arabidopsis thaliana to modify nuclear transcription regulators DELLAs, revealing a new regulatory mechanism for gene expression. The paralog of AtSPY, SECRET AGENT (SEC), is an O-link-N-acetylglucosamine (GlcNAc) transferase (OGT), which O-GlcNAcylates Ser/Thr residues of target proteins. Both AtSPY and AtSEC are tetratricopeptide repeat-domain-containing glycosyltransferases in the GT41 family. The discovery that AtSPY is a POFUT clarified decades of miss-classification of AtSPY as an OGT. SPY and SEC play pleiotropic roles in plant development, and the interactions between SPY and SEC are complex. SPY-like genes are conserved in diverse organisms, except in fungi and metazoans, suggesting that O-fucosylation is a common mechanism in modulating intracellular protein functions.},
doi = {10.1016/j.sbi.2020.12.013},
journal = {Current Opinion in Structural Biology},
number = C,
volume = 68,
place = {United States},
year = {Mon Jan 18 00:00:00 EST 2021},
month = {Mon Jan 18 00:00:00 EST 2021}
}

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