Cited by 429Plant Molecular Biology ResearchPlant Parasitism and ResistanceLight effects on plants

MAX2 participates in an SCF complex which acts locally at the node to suppress shoot branching

Stirnberg, Petra, Furner, Ian J., Ottoline Leyser, H. M.·2007·The Plant Journal

Abstract

Summary: The Arabidopsis gene ORE9/MAX2 encodes an F‐box leucine‐rich repeat protein. F‐box proteins function as the substrate‐recruiting subunit of SCF‐type ubiquitin E3 ligases in protein ubiquitination. One of several phenotypes of max2 mutants, the highly branched shoot, is identical to mutants at three other MAX loci. Reciprocal grafting, double mutant analysis and gene cloning suggest that all MAX genes act in a common pathway, where branching suppression depends on MAX2 activity in the shoot, in response to an acropetally mobile signal that requires MAX3, MAX4 and MAX1 for its production. Here, we further investigate the site and mode of action of MAX2 in branching. Transcript analysis and a translational MAX2–GUS fusion indicate that MAX2 is expressed throughout the plant, most highly in developing vasculature, and is nuclear‐localized in many cell types. Analysis of cell autonomy shows that MAX2 acts locally, either in the axillary bud, or in adjacent stem or petiole tissue. Expression of MAX2 from the CaMV 35S promoter complements the max2 mutant, does not affect branching in a wild‐type background and partially rescues increased branching in the max1, max3 and max4 backgrounds. Expression of mutant MAX2, lacking the F‐box domain, under the CaMV 35S promoter does not complement max2, and dominant‐negatively affects branching in the wild‐type background. Myc‐epitope‐tagged MAX2 interacts with the core SCF subunits ASK1 and AtCUL1 in planta. We conclude that axillary shoot growth is controlled locally, at the node, by an SCF MAX2, the action of which is enhanced by the mobile MAX signal.

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Crossref · 10.1111/j.1365-313x.2007.03032.x

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  • Grafting experiments revealed a class of SL response mutants that could not be complemented by wild type rootstocks, indicating a role in SL perception and signaling rather than biosynthesis.

    “Grafting experiments also revealed a class of SL response mutants that could not be complemented by wild type rootstocks (Beveridge et al., 1996; Stirnberg et al., 2007), indicating a role in SL perception and signaling rather than biosynthesis.”

    From Shaping plant architecture (2015) · cites this paper as Stirnberg et al., 2007

  • The Arabidopsis max2 mutant encodes an F-box protein involved in SL signaling.

    “An example is the Arabidopsis max2 mutant (Stirnberg et al., 2007) that encodes an F-box protein involved in SL signaling.”

    From Shaping plant architecture (2015) · cites this paper as Stirnberg et al., 2007

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Authors
Stirnberg, P., Furner, I. J., & Ottoline Leyser, H. M.
Affiliations
  • University of York (GB)
  • University of Cambridge (GB)
Venue
The Plant Journal
Publisher
Wiley
Published
2007-03-05
Volume
50
Issue
1
Pages
80-94
ISSN
  • 0960-7412 (ISSN-L)
  • 1365-313X
OpenAlex
W1927613538
Cited by
429
References
8
Citations by year
2026: 13 · 2025: 15 · 2024: 17 · 2023: 16 · 2022: 31 · 2021: 18 · 2020: 19 · 2019: 26 · 2018: 22 · 2017: 31 · 2016: 20 · 2015: 30 · 2014: 21 · 2013: 37 · 2012: 33
FWCI
23.09
Type
journal article
Language
en
Open access
closed
Locations
  • The Plant Journal (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Parasitism and Resistance
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
Keywords
MAX2, F-box protein, SCF ubiquitin ligase, axillary buds, leucine-rich repeat proteins, cell autonomy, ASK1, ubiquitination, Arabidopsis thaliana
MeSH terms
Carrier Proteins, Protein Binding, Arabidopsis, Gene Expression Regulation, Plant, Plant Shoots, Arabidopsis Proteins, SKP Cullin F-Box Protein Ligases, Immunoprecipitation

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