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/


  • eng