Novel nucleocytoplasmic protein O-fucosylation by SPINDLY regulates diverse developmental processes in plants.
Journal Article (Review;Journal Article)
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.
Full Text
Duke Authors
Cited Authors
- Sun, T-P
Published Date
- June 2021
Published In
Volume / Issue
- 68 /
Start / End Page
- 113 - 121
PubMed ID
- 33476897
Pubmed Central ID
- PMC8222059
Electronic International Standard Serial Number (EISSN)
- 1879-033X
International Standard Serial Number (ISSN)
- 0959-440X
Digital Object Identifier (DOI)
- 10.1016/j.sbi.2020.12.013
Language
- eng