SAUR63 stimulates cell growth at the plasma membrane
Nagpal, Punita (Université de Lyon. Laboratoire Reproduction et Développement des Plantes)
Reeves, Paul (University of North Carolina at Chapel Hill. Department of Biology)
Wong, Jeh Haur (University of Minnesota. Department of Plant and Microbial Biology)
Armengot, Laia (Centre de Recerca en Agrigenòmica)
Chae, Keun (University of North Carolina at Chapel Hill. Department of Biology)
Rieveschl, Nathaniel (University of North Carolina at Chapel Hill. Department of Biology)
Trinidad, Brendan (University of North Carolina at Chapel Hill. Department of Biology)
Davidsdottir, Vala (University of North Carolina at Chapel Hill. Department of Biology)
Jain, Prateek (University of North Carolina at Chapel Hill. Department of Biology)
Gray, William (University of Minnesota. Department of Plant and Microbial Biology)
Jaillais, Yvon (Université de Lyon. Laboratoire Reproduction et Développement des Plantes)
Reed, Jason (Université de Lyon. Laboratoire Reproduction et Développement des Plantes)

Data:	2022
Resum:	In plants, regulated cell expansion determines organ size and shape. Several members of the family of redundantly acting Small Auxin Up RNA (SAUR) proteins can stimulate plasma membrane (PM) H+-ATPase proton pumping activity by inhibiting PM-associated PP2C. D phosphatases, thereby increasing the PM electrochemical potential, acidifying the apoplast, and stimulating cell expansion. Similarly, Arabidopsis thaliana SAUR63 was able to increase growth of various organs, antagonize PP2C. D5 phosphatase, and increase H+-ATPase activity. Using a gain-of-function approach to bypass genetic redundancy, we dissected structural requirements for SAUR63 growth-promoting activity. The divergent N-terminal domain of SAUR63 has a predicted basic amphipathic á-helix and was able to drive partial PM association. Deletion of the N-terminal domain decreased PM association of a SAUR63 fusion protein, as well as decreasing protein level and eliminating growth-promoting activity. Conversely, forced PM association restored ability to promote H+-ATPase activity and cell expansion, indicating that SAUR63 is active when PM-associated. Lipid binding assays and perturbations of PM lipid composition indicate that the N-terminal domain can interact with PM anionic lipids. Mutations in the conserved SAUR domain also reduced PM association in root cells. Thus, both the N-terminal domain and the SAUR domain may cooperatively mediate the SAUR63 PM association required to promote growth.
Ajuts:	European Commission 615739 European Research Council 3363360
Drets:	Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.
Llengua:	Anglès
Document:	Article ; recerca ; Versió publicada
Matèria:	Arabidopsis ; Arabidopsis Proteins ; Cell Membrane ; Gene Expression Regulation, Plant ; Indoleacetic Acids ; Lipids ; Phosphoric Monoester Hydrolases ; Proton-Translocating ATPases ; Protons ; RNA
Publicat a:	PLoS Genetics, Vol. 18, Num. 9 (September 2022) , art. e1010375, ISSN 1553-7404

DOI: 10.1371/journal.pgen.1010375
PMID: 36121899

33 p, 5.0 MB

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