Seed longevity is controlled by metacaspases

Chen Liu, Ioannis H. Hatzianestis, Thorsten Pfirrmann, Salim H. Reza, Elena A. Minina, Ali Moazzami, Simon Stael, Emilio Gutierrez–Beltran, Eugenia Pitsili, Peter Dörmann, Sabine D’Andrea, Kris Gevaert, Francisco Romero–Campero, Pingtao Ding, Moritz K. Nowack, Frank Breusegem, Jonathan D. G. Jones, Peter V. Bozhkov and Panagiotis N. Moschou ()
Additional contact information
Chen Liu: Sun Yat–Sen University
Ioannis H. Hatzianestis: University of Crete
Thorsten Pfirrmann: Health and Medical University
Salim H. Reza: Uppsala University
Elena A. Minina: Swedish University of Agricultural Sciences and Linnean Center for Plant Biology
Ali Moazzami: Swedish University of Agricultural Sciences and Linnean Center for Plant Biology
Simon Stael: Swedish University of Agricultural Sciences and Linnean Center for Plant Biology
Emilio Gutierrez–Beltran: Consejo Superior de Investigaciones Cientıficas (CSIC)–Universidad de Sevilla
Eugenia Pitsili: Technologiepark 71
Peter Dörmann: Institute of Molecular Physiology and Biotechnology of Plants (IMBIO)
Sabine D’Andrea: Institut Jean–Pierre Bourgin (IJPB)
Kris Gevaert: VIB Center for Medical Biotechnology
Francisco Romero–Campero: Consejo Superior de Investigaciones Cientıficas (CSIC)–Universidad de Sevilla
Pingtao Ding: Leiden University
Moritz K. Nowack: Technologiepark 71
Frank Breusegem: Technologiepark 71
Jonathan D. G. Jones: University of East Anglia
Peter V. Bozhkov: Swedish University of Agricultural Sciences and Linnean Center for Plant Biology
Panagiotis N. Moschou: University of Crete

Nature Communications, 2024, vol. 15, issue 1, 1-17

Abstract: Abstract To survive extreme desiccation, seeds enter a period of quiescence that can last millennia. Seed quiescence involves the accumulation of protective storage proteins and lipids through unknown adjustments in protein homeostasis (proteostasis). Here, we show that mutation of all six type–II metacaspase (MCA–II) proteases in Arabidopsis thaliana disturbs proteostasis in seeds. MCA–II mutant seeds fail to restrict the AAA ATPase CELL DIVISION CYCLE 48 (CDC48) at the endoplasmic reticulum to discard misfolded proteins, compromising seed storability. Endoplasmic reticulum (ER) localization of CDC48 relies on the MCA–IIs-dependent cleavage of PUX10 (ubiquitination regulatory X domain–containing 10), the adaptor protein responsible for titrating CDC48 to lipid droplets. PUX10 cleavage enables the shuttling of CDC48 between lipid droplets and the ER, providing an important regulatory mechanism sustaining spatiotemporal proteolysis, lipid droplet dynamics, and protein homeostasis. In turn, the removal of the PUX10 adaptor in MCA–II mutant seeds partially restores proteostasis, CDC48 localization, and lipid droplet dynamics prolonging seed lifespan. Taken together, we uncover a proteolytic module conferring seed longevity.

Date: 2024
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DOI: 10.1038/s41467-024-50848-2

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