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SHOU4/4L proteins are crucial for plant immunity against pathogens. Their reversible phosphorylation by BOTRYTIS-INDUCED KINASE 1 regulates plant development and pathogen resistance by affecting cellulose synthesis.

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Area of Science:

  • Plant immunity
  • Molecular plant-microbe interactions
  • Signal transduction

Background:

  • Pattern recognition receptors (PRRs) initiate pattern-triggered immunity (PTI) by sensing molecular patterns.
  • Receptor-like cytoplasmic kinases (RLCKs) are key signaling components downstream of PRRs, regulating plant defense responses through protein phosphorylation.
  • Understanding RLCK substrates is vital for elucidating plant immune mechanisms.

Purpose of the Study:

  • To identify and characterize RLCK-regulated substrate proteins involved in plant immunity.
  • To investigate the role of SHOU4 and SHOU4L in plant resistance to pathogens.
  • To elucidate the regulatory mechanism of SHOU4L by RLCKs.

Main Methods:

  • Phosphorylation analysis of SHOU4 and SHOU4L upon pattern elicitation.
  • Protein-protein interaction studies using co-immunoprecipitation.
  • Phosphoproteomic analysis to identify phosphorylation sites.
  • Functional analysis of SHOU4L variants in loss-of-function mutants.

Main Results:

  • SHOU4 and SHOU4L are rapidly phosphorylated upon pattern elicitation and are essential for resistance to bacterial and fungal pathogens.
  • BOTRYTIS-INDUCED KINASE 1 (BIK1), an RLCK-VII kinase, interacts with and phosphorylates SHOU4L.
  • Reversible phosphorylation of SHOU4L is critical for both plant immunity and development, influencing its interaction with Cellulose Synthase 1 (CESA1).

Conclusions:

  • SHOU4/4L are newly identified components of pattern-triggered immunity (PTI).
  • BIK1-mediated phosphorylation of SHOU4L regulates plant immunity and development by modulating its interaction with CESA1 and cellulose synthesis.
  • This study reveals a novel mechanism of plant immune signaling involving RLCK regulation of substrate protein function.