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

Journal Article · · Current Opinion in Structural Biology
 [1]
  1. Duke Univ., Durham, NC (United States)

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.

Research Organization:
Duke Univ., Durham, NC (United States)
Sponsoring Organization:
USDOE Office of Science (SC); National Institutes of Health (NIH); National Science Foundation (NSF); USDA
Grant/Contract Number:
SC0019393; 2R01 GM100051-05A1; MCB-1818161; 2018-67013-27395
OSTI ID:
1853182
Alternate ID(s):
OSTI ID: 1778488
Journal Information:
Current Opinion in Structural Biology, Vol. 68, Issue C; ISSN 0959-440X
Publisher:
ElsevierCopyright Statement
Country of Publication:
United States
Language:
English

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