Publications [#370022] of Tai-ping Sun
search PubMed.Papers Published
- Kumar, S; Wang, Y; Zhou, Y; Dillard, L; Li, F-W; Sciandra, CA; Sui, N; Zentella, R; Zahn, E; Shabanowitz, J; Hunt, DF; Borgnia, MJ; Bartesaghi, A; Sun, T-P; Zhou, P, Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY.,
Nat Commun, vol. 14 no. 1
(March, 2023),
pp. 1538 [doi] .
(last updated on 2024/11/02)Abstract:
SPINDLY (SPY) in Arabidopsis thaliana is a novel nucleocytoplasmic protein O-fucosyltransferase (POFUT), which regulates diverse developmental processes. Sequence analysis indicates that SPY is distinct from ER-localized POFUTs and contains N-terminal tetratricopeptide repeats (TPRs) and a C-terminal catalytic domain resembling the O-linked-N-acetylglucosamine (GlcNAc) transferases (OGTs). However, the structural feature that determines the distinct enzymatic selectivity of SPY remains unknown. Here we report the cryo-electron microscopy (cryo-EM) structure of SPY and its complex with GDP-fucose, revealing distinct active-site features enabling GDP-fucose instead of UDP-GlcNAc binding. SPY forms an antiparallel dimer instead of the X-shaped dimer in human OGT, and its catalytic domain interconverts among multiple conformations. Analysis of mass spectrometry, co-IP, fucosylation activity, and cryo-EM data further demonstrates that the N-terminal disordered peptide in SPY contains trans auto-fucosylation sites and inhibits the POFUT activity, whereas TPRs 1-5 dynamically regulate SPY activity by interfering with protein substrate binding.