Proteomics

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SNC1 phosphorylation sites invivo LC-MSMS

ABSTRACT: Toll/interleukin-1 receptor (TIR) domain proteins are immune signaling components and function as NAD+-cleaving enzymes to activate defense responses. Activation of TIRs represses growth and drives cell death in plants and promotes axon degeneration in animals, but how plant TIRs are repressed remains unclear. Here, we show that TIR NADase activity requires a conserved serine residue spatially close to the catalytic glutamate. The plant Ca2+-dependent protein kinases (CPKs), the mammalian Ca2+/calmodulin-dependent protein kinase II delta (CAMK2D) and TANK binding kinase 1 (TBK1) phosphorylate TIR domains at this conserved serine, which blocks TIR NADase activities and functions and thus maintains growth in plants and suppresses SARM1 TIR signaling in animals, respectively. Our findings define a fundamental molecular mechanism by which phosphorylation at a conserved serine residue blocks TIR signaling to balance growth and defense trade-offs.

INSTRUMENT(S):

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

SUBMITTER: Bo Yu  

LAB HEAD: Yang Zhao

PROVIDER: PXD060129 | Pride | 2025-06-12

REPOSITORIES: Pride

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20231206_095344_D20231150_DirectDIA_Phospho_20231206_Report_pro.tsv Tabular
20231206_095358_D20231150_DirectDIA_Phospho_20231206_Report_pep.tsv Tabular
20231206_095406_D20231150_DirectDIA_Phospho_20231206_Report_mod.tsv Tabular
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Publications

TIR immune signalling is blocked by phosphorylation to maintain plant growth.

Li Jun J   Chen Sisi S   Yu Bo B   Li Qingzhong Q   Liu Ruijia R   Wang Zaiqing Z   Wan Li L   Zhao Yang Y  

Nature plants 20250609 6

Toll/interleukin-1 receptor (TIR) domain proteins are immune signalling components and function as NAD<sup>+</sup>-cleaving enzymes to activate defence responses. In plants, TIR activation triggers cell death and severely represses growth, especially under osmotic stress, while in animals, it promotes axon degeneration. However, the mechanisms regulating TIR suppression remain unclear. Here we show that TIR NADase activity requires a conserved serine residue spatially close to the catalytic glut  ...[more]

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