ArticlePLoS genetics2022
SAUR63 stimulates cell growth at the plasma membrane.
Article in PLoS genetics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
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- A PIF-SAUR module safeguards hypocotyl elongation from ABA inhibition in the dark.Science advances · 2025Article
- PtrSAUR32 Interacts with PtrPP2C.Ds to Regulate Root Growth in Citrus.Plants (Basel, Switzerland) · 2025Article
- The apoplastic pH is a key determinant in the hypocotyl growth response to auxin dosage and light.Nature plants · 2025Article
- Expression of a mammalian RNA demethylase increases flower number and floral stem branching inPlant direct · 2024Article
- Meta-analysis of public RNA sequencing data of abscisic acid-related abiotic stresses inFrontiers in plant science · 2024Article
- Plant extracellular self-DNA inhibits growth and induces immunity via the jasmonate signaling pathway.Plant physiology · 2023Article
- Genome-Wide Identification and Functional Analysis of the Roles ofInternational journal of molecular sciences · 2023Article
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Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
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 α-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.
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