2. Academic Validation
  3. A lineage-specific selective autophagy receptor module mediates P-body turnover

A lineage-specific selective autophagy receptor module mediates P-body turnover

  • Dev Cell. 2026 Apr 8;61(4):744-759.e11. doi: 10.1016/j.devcel.2026.01.017.
Alibek Abdrakhmanov 1,  Elizabeth Ethier 2,  Aleksandra S Anisimova 2,  Nenad Grujic 3,  Ranjith K Papareddy 4,  Marion Clavel 5,  G Elif Karagöz 6,  Erinc Hallacli 7,  Yasin Dagdas 8
Affiliations

Affiliations

  • 1 Gregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria; Vienna BioCenter PhD Program, Doctoral School of the University of Vienna and Medical University of Vienna, 1030 Vienna, Austria.
  • 2 Vienna BioCenter PhD Program, Doctoral School of the University of Vienna and Medical University of Vienna, 1030 Vienna, Austria; Max Perutz Labs, Medical University of Vienna, Vienna BioCenter (VBC), Vienna, Austria.
  • 3 Gregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
  • 4 Gregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria; Heidelberg University, Centre for Organismal Studies (COS), 69120 Heidelberg, Germany.
  • 5 Max-Planck-Institut für Molekulare Pflanzenphysiologie, Potsdam, Golm, Germany.
  • 6 Max Perutz Labs, Medical University of Vienna, Vienna BioCenter (VBC), Vienna, Austria.
  • 7 Max Perutz Labs, Medical University of Vienna, Vienna BioCenter (VBC), Vienna, Austria. Electronic address: [email protected].
  • 8 Gregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria; Heidelberg University, Centre for Organismal Studies (COS), 69120 Heidelberg, Germany. Electronic address: [email protected].
PMID: 41734762 DOI: 10.1016/j.devcel.2026.01.017
Abstract

Processing bodies (P-bodies) are conserved ribonucleoprotein granules central to RNA metabolism across eukaryotes. Although the mechanisms underlying their assembly are well understood, the pathways governing their selective turnover remain unclear. Here, we identify the conserved decapping proteins Enhancer of mRNA decapping 4 (EDC4) and decapping protein 1 (DCP1) as a selective Autophagy receptor pair responsible for P-body turnover in the model plant Marchantia polymorpha. MpEDC4 engages ATG8 via a canonical ATG8-interacting motif, while MpDCP1 contains a previously unrecognized reverse ATG8-interacting motif within its intrinsically disordered region. Mutations disrupting these motifs impair the autophagic degradation of P-bodies, demonstrating a cooperative receptor mechanism. Notably, this autophagic function is lineage-specific, as orthologs in Arabidopsis and humans lack ATG8-binding capacity. Strikingly, the heterologous expression of MpEDC4 in human cells promotes the degradation of α-synuclein, a protein linked to Parkinson's disease etiology. Our findings uncover an evolutionary innovation that links RNA metabolism to selective Autophagy and open avenues for the cross-kingdom engineering of targeted protein degradation pathways.

Keywords

ATG8; Marchantia; P-body; RNP-granules; autophagic flux; receptor engineering; selective autophagy; selective autophagy receptor; targeted protein degradation; α-synuclein degradation.

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