| Autor: |
Marie-Dominique Jolivet, Paul Gouguet, Anthony Legrand, Kaltra Xhelilaj, Natalie Faiss, Aurélie Massoni-Laporte, Terezinha Robbe, Isabelle Sagot, Marie Boudsocq, Sylvie German-Retana, Suayib Üstün, Antoine Loquet, Birgit Habenstein, Véronique Germain, Sébastien Mongrand, Julien Gronnier |
| Rok vydání: |
2023 |
| DOI: |
10.1101/2023.01.25.525625 |
| Popis: |
The dynamic regulation of the plasma membrane (PM) organization at the nanoscale emerged as a key element shaping the outcome of host-microbe interactions. Protein organization into nanodomains (ND) is often assumed to be linked to the activation of cellular processes. In contrast, we have previously shown that the phosphorylation of theSolanum tuberosumREM1.3 (StREM1.3) N-terminal domain disperses its native ND organization and promotes its inhibitory effect onPotato Virus X(PVX) cell-to-cell movement. Here, we show that the phosphorylation of StREM1.3 modify the chemical environment of numerous residues in its intrinsically-disordered N-terminal domain. We leveraged exploratory screens to identify potential phosphorylation-dependent interactors of StREM1.3. Herewith, we uncovered uncharacterized regulators of PVX cell-to-cell movement, linking StREM1.3 to autophagy, water channels and the actin cytoskeleton. We show that theSolanum tuberosumactin depolymerizing factors 2 (StADF2) alters StREM1.3 NDs and limits PVX cell-to-cell movement in a REMORIN-dependent manner. Mutating a conserved single residue reported to affect ADFs affinity to actin inhibits StADF2 effect on StREM1.3 ND organization and PVX cell-to-cell movement. These observations provide functional links between the organization of plant PM and the actin cytoskeleton and suggests that the alteration of StREM1.3 ND organization promotes plant anti-viral responses. We envision that analogous PM re-organization applies for additional signaling pathways in plants and in other organisms. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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