Novel nucleocytoplasmic protein O-fucosylation by SPINDLY regulates diverse developmental processes in plants.
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.
Duke Scholars
Published In
DOI
EISSN
ISSN
Publication Date
Volume
Start / End Page
Related Subject Headings
- Repressor Proteins
- Protein Processing, Post-Translational
- N-Acetylglucosaminyltransferases
- Glycosylation
- Biophysics
- Arabidopsis Proteins
- Arabidopsis
- Acetylglucosamine
- 3101 Biochemistry and cell biology
- 0601 Biochemistry and Cell Biology
Citation
Published In
DOI
EISSN
ISSN
Publication Date
Volume
Start / End Page
Related Subject Headings
- Repressor Proteins
- Protein Processing, Post-Translational
- N-Acetylglucosaminyltransferases
- Glycosylation
- Biophysics
- Arabidopsis Proteins
- Arabidopsis
- Acetylglucosamine
- 3101 Biochemistry and cell biology
- 0601 Biochemistry and Cell Biology