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Main conclusion <p>OsPP2C10, a member of the OsPP2C subclass F2, is localized at the endoplasmic reticulum exit sites and interacts with vesicle trafficking components, OsSAR1C and an OsPHYTOLONGIN. Altered accumulation patterns of TLP and GLU2 proteins in the apoplast of <i>OsPP2C10 </i>knockout, knockdown, and overexpression lines suggest potential regulatory roles of OsPP2C10 in protein vesicle trafficking.</p> Abstract <p>Protein phosphatase 2Cs (PP2Cs) are key regulators of signal transduction that act through dephosphorylation of target proteins. To identify PP2Cs functioning on membranous organelles in rice (<i>Oryza sativa</i>), we screened all 78 OsPP2Cs and found that OsPP2C10 possesses a functional N-terminal transmembrane domain and is localized at the endoplasmic reticulum exit site. OsPP2C10 interacts with OsSAR1C, a component of the COPII complex, and OsPHYTOLONGIN, a VAMP72 longin-related protein, both of which are essential regulators of vesicle trafficking. Functional analysis using T-DNA knockout, RNAi knockdown, and overexpression lines revealed that OsPP2C10 influences the accumulation of secretory proteins such as TLP/PR5 and GLU2/PR2 in the apoplast. These findings suggest potential regulatory roles of OsPP2C10 in protein trafficking in rice.</p>

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Rice protein phosphatase 2C10 (OsPP2C10) interacts with vesicle trafficking components and functions in the regulation of protein vesicle trafficking in rice

  • 期刊论文

  • 发表日期：

    2025年12月9日

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  • Myung Ki Min,
  • Sangkyu Park,
  • Kyeyoon Lee,
  • Jaeeun Song,
  • Saet Buyl Lee,
  • Hyo Lee,
  • Sangchul Choi,
  • Suntae Kim,
  • Beom-Gi Kim

摘要

Main conclusion

OsPP2C10, a member of the OsPP2C subclass F2, is localized at the endoplasmic reticulum exit sites and interacts with vesicle trafficking components, OsSAR1C and an OsPHYTOLONGIN. Altered accumulation patterns of TLP and GLU2 proteins in the apoplast of OsPP2C10 knockout, knockdown, and overexpression lines suggest potential regulatory roles of OsPP2C10 in protein vesicle trafficking.

Abstract

Protein phosphatase 2Cs (PP2Cs) are key regulators of signal transduction that act through dephosphorylation of target proteins. To identify PP2Cs functioning on membranous organelles in rice (Oryza sativa), we screened all 78 OsPP2Cs and found that OsPP2C10 possesses a functional N-terminal transmembrane domain and is localized at the endoplasmic reticulum exit site. OsPP2C10 interacts with OsSAR1C, a component of the COPII complex, and OsPHYTOLONGIN, a VAMP72 longin-related protein, both of which are essential regulators of vesicle trafficking. Functional analysis using T-DNA knockout, RNAi knockdown, and overexpression lines revealed that OsPP2C10 influences the accumulation of secretory proteins such as TLP/PR5 and GLU2/PR2 in the apoplast. These findings suggest potential regulatory roles of OsPP2C10 in protein trafficking in rice.