4.8 Article

Plant ESCRT protein ALIX coordinates with retromer complex in regulating receptor-mediated sorting of soluble vacuolar proteins

Publisher

NATL ACAD SCIENCES
DOI: 10.1073/pnas.2200492119

Keywords

vacuolar trafficking; endosomal recycling; multivesicular body/prevacuolar compartment (MVB/PVC); ESCRT machiner; retromer complex

Funding

  1. National Natural Science Foundation of China [31870171, 32061160467, 31970181, 32170342]
  2. Zhejiang Provincial Natural Science Foundation of China [LR20C020001]
  3. Fundamental Research Funds for the Provincial Universities of Zhejiang [2020KJ001]
  4. Research Grants Council of Hong Kong [R4005-18, AoE/M-05/12, C4012-16E, C4033-19E, C4002-17G]
  5. Zhejiang AF University [2018FR029]
  6. 111 Project [D18008]
  7. China Postdoctoral Science Foundation [2020M681919]
  8. NSFC [31670179, 91854201]
  9. Japan Society for the Promotion of Science [15H05776]
  10. Hirao Taro Foundation of KONAN GAKUEN for Academic Research
  11. Fok Ying-Tong Education Foundation for Young Teachers [171014]
  12. MCIN/AEI/FEDER una manera de hacer Europa [PGC2018-094257-B-C21]

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This study elucidates the role and mechanism of ALIX in regulating vacuolar transport of soluble proteins in plants. It is found that ALIX physically interacts with the retromer core subunits Vps26 and Vps29 and cooperatively regulates the trafficking of soluble vacuolar proteins. Depletion of ALIX disrupts the membrane recruitment of Vps26 and Vps29 and alters the endosomal localization of vacuolar sorting receptors.
Vacuolar proteins play essential roles in plant physiology and development, but the factors and the machinery regulating their vesicle trafficking through the endomembrane compartments remain largely unknown. We and others have recently identified an evolutionarily conserved plant endosomal sorting complex required for transport (ESCRT)-associated protein apoptosis-linked gene-2 interacting protein X (ALIX), which plays canonical functions in the biogenesis of the multivesicular body/prevacuolar compartment (MVB/PVC) and in the sorting of ubiquitinated membrane proteins. In this study, we elucidate the roles and underlying mechanism of ALIX in regulating vacuolar transport of soluble proteins, beyond its conventional ESCRT function in eukaryotic cells. We show that ALIX colocalizes and physically interacts with the retromer core subunits Vps26 and Vps29 in planta. Moreover, double-mutant analysis reveals the genetic interaction of ALIX with Vps26 and Vps29 for regulating trafficking of soluble vacuolar proteins. Interestingly, depletion of ALIX perturbs membrane recruitment of Vps26 and Vps29 and alters the endosomal localization of vacuolar sorting receptors (VSRs). Taken together, ALIX functions as a unique retromer core subcomplex regulator by orchestrating receptor-mediated vacuolar sorting of soluble proteins.

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