Evidence map›Paper›PMID 35984304›Full record

ArticlePlant physiology2022

The START domain mediates Arabidopsis GLABRA2 dimerization and turnover independently of homeodomain DNA binding.

Thiya Mukherjee, Bibek Subedi, Aashima Khosla, Erika M Begler, Preston M Stephens, Adara L Warner, Ruben Lerma-Reyes, Kyle A Thompson, Sumedha Gunewardena, Kathrin Schrick

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
4.0field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 21 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Thiya MukherjeeDivision of Biology, Kansas State University, Manhattan, Kansas 66506, USA.ORCID 0000-0003-4053-4501
Bibek SubediDivision of Biology, Kansas State University, Manhattan, Kansas 66506, USA.ORCID 0000-0002-3105-5616
Aashima KhoslaDivision of Biology, Kansas State University, Manhattan, Kansas 66506, USA.ORCID 0000-0001-8533-4269
Erika M BeglerDivision of Biology, Kansas State University, Manhattan, Kansas 66506, USA.ORCID 0000-0002-6459-7446
Preston M StephensDivision of Biology, Kansas State University, Manhattan, Kansas 66506, USA.ORCID 0000-0002-4767-0939
Adara L WarnerDivision of Biology, Kansas State University, Manhattan, Kansas 66506, USA.
Ruben Lerma-ReyesDivision of Biology, Kansas State University, Manhattan, Kansas 66506, USA.ORCID 0000-0003-3987-3565
Kyle A ThompsonDivision of Biology, Kansas State University, Manhattan, Kansas 66506, USA.ORCID 0000-0002-2827-7680
Sumedha GunewardenaDepartment of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, Kansas 66160, USA.ORCID 0000-0003-2097-135X
Kathrin SchrickDivision of Biology, Kansas State University, Manhattan, Kansas 66506, USA.ORCID 0000-0001-8006-5944
Kansas State University · USUniversity of California, Riverside · USUniversity of Kansas Medical Center · US

Funding

Mentoring CoreP20GM103418 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI Douglas E Wright · 2012 to 2026
$63.0M
TRANSEPITHELIAL ION TRANSPORT &ITS REGULATIONP20RR017686 · NCRR · KANSAS STATE UNIVERSITY · PI MELGAREJO GARCIA, LUIS TONATIUH · 2002 to 2011
$21.8M
NCRR NIH HHS P20 RR017686NIGMS NIH HHS P20 GM103418
6 · The paper itself

Abstract

Class IV homeodomain leucine-zipper transcription factors (HD-Zip IV TFs) are key regulators of epidermal differentiation that are characterized by a DNA-binding HD in conjunction with a lipid-binding domain termed steroidogenic acute regulatory-related lipid transfer (START). Previous work established that the START domain of GLABRA2 (GL2), a HD-Zip IV member from Arabidopsis (Arabidopsis thaliana), is required for TF activity. Here, we addressed the functions and possible interactions of START and the HD in DNA binding, dimerization, and protein turnover. Deletion analysis of the HD and missense mutations of a conserved lysine (K146) resulted in phenotypic defects in leaf trichomes, root hairs, and seed mucilage, similar to those observed for START domain mutants, despite nuclear localization of the respective proteins. In vitro and in vivo experiments demonstrated that while HD mutations impair binding to target DNA, the START domain is dispensable for DNA binding. Vice versa, protein interaction assays revealed impaired GL2 dimerization for multiple alleles of START mutants, but not HD mutants. Using in vivo cycloheximide chase experiments, we provided evidence for the role of START, but not HD, in maintaining protein stability. This work advances our mechanistic understanding of HD-Zip TFs as multidomain regulators of epidermal development in plants.

Indexed as

ArabidopsisArabidopsis ProteinsDimerizationDNAGene Expression Regulation, PlantHomeodomain ProteinsLeucine ZippersLipidsArabidopsis ProteinsDNAHomeodomain ProteinsLipids

Identifiers

PMID35984304
PMCPMC9706451
OpenAlexW4294349274

What OpenQuestion holds

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Registered trials

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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.