Evidence map›Paper›PMID 24492333›Full record

ArticlePlant physiology2014

Revisiting the evolutionary history and roles of protein phosphatases with Kelch-like domains in plants.

Gustavo A Maselli, Claudio H Slamovits, Javier I Bianchi, Josep Vilarrasa-Blasi, Ana I Caño-Delgado, Santiago Mora-García

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Article in Plant physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

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27citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

27 citing papers in PubMed.

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  12. Regulation of Three Key Kinases of Brassinosteroid Signaling Pathway.International journal of molecular sciences · 2020
    Review
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

6 authors.

Gustavo A MaselliFundación Instituto Leloir and Instituto de Investigaciones Bioquímicas de Buenos Aires-Consejo Nacional de Investigaciones Científicas y Técnicas, C1405BWE Buenos Aires, Argentina.
Claudio H Slamovits
Javier I Bianchi
Josep Vilarrasa-Blasi
Ana I Caño-Delgado
Santiago Mora-García

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein phosphatases with Kelch-like domains (PPKL) are members of the phosphoprotein phosphatases family present only in plants and alveolates. PPKL have been described as positive effectors of brassinosteroid (BR) signaling in plants. Most of the evidence supporting this role has been gathered using one of the four homologs in Arabidopsis (Arabidopsis thaliana), brassinosteroid-insensitive1 suppressor (BSU1). We reappraised the roles of the other three members of the family, BSL1, BSL2, and BSL3, through phylogenetic, functional, and genetic analyses. We show that BSL1 and BSL2/BSL3 belong to two ancient evolutionary clades that have been highly conserved in land plants. In contrast, BSU1-type genes are exclusively found in the Brassicaceae and display a remarkable sequence divergence, even among closely related species. Simultaneous loss of function of the close paralogs BSL2 and BSL3 brings about a peculiar array of phenotypic alterations, but with marginal effects on BR signaling; loss of function of BSL1 is, in turn, phenotypically silent. Still, the products of these three genes account for the bulk of PPKL-related activity in Arabidopsis and together have an essential role in the early stages of development that BSU1 is unable to supplement. Our results underline the functional relevance of BSL phosphatases in plants and suggest that BSL2/BSL3 and BSU1 may have contrasting effects on BR signaling. Given that BSU1-type genes have likely undergone a functional shift and are phylogenetically restricted, we caution that inferences based on these genes to the whole family or to other species may be misleading.

Indexed as

Evolution, MolecularArabidopsisBrassinosteroidsFlowersGene Expression Regulation, PlantGenes, PlantMutationPhenotypePhosphoprotein PhosphatasesPhylogenyPlant ProteinsPlantsProtein Structure, TertiarySignal TransductionSubcellular FractionsBrassinosteroidsPhosphoprotein PhosphatasesPlant Proteins

Identifiers

PMID24492333
PMCPMC3938638

What OpenQuestion holds

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.