Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation (Q27681449)

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English	Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation	scientific article

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instance of

scholarly article

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title

Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation (English)

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main subject

cell biology

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crystal structure

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phosphorylation

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brassinosteroid

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based on heuristic

inferred from title

author

Michael Hothorn

series ordinal

6

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Daniel Bojar

object named as

Daniel Bojar

series ordinal

1

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Julia Santiago

object named as

Julia Santiago

series ordinal

3

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Richard Bayliss

object named as

Richard Bayliss

series ordinal

5

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author name string

Jacobo Martinez

series ordinal

2

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Vladimir Rybin

series ordinal

4

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publication date

April 2014

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published in

The Plant Journal

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volume

78

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issue

1

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page(s)

31-43

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cites work

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Transphosphorylation of E. coli Proteins during Production of Recombinant Protein Kinases Provides a Robust System to Characterize Kinase Specificity.

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Tyrosine Phosphorylation of the BRI1 Receptor Kinase Occurs via a Post-Translational Modification and is Activated by the Juxtamembrane Domain

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Autophosphorylation of Tyr-610 in the receptor kinase BAK1 plays a role in brassinosteroid signaling and basal defense gene expression.

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Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a component of brassinosteroid signaling in Arabidopsis

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The Arabidopsis thaliana brassinosteroid receptor (AtBRI1) contains a domain that functions as a guanylyl cyclase in vitro.

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Brassinosteroids regulate dissociation of BKI1, a negative regulator of BRI1 signaling, from the plasma membrane

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Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts Agrobacterium-mediated transformation.

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The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 protein complex includes BRASSINOSTEROID-INSENSITIVE1.

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Stomatal patterning and differentiation by synergistic interactions of receptor kinases

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Biosynthesis and metabolism of brassinosteroids

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BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling

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29 September 2017

BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling

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Receptor-like kinases from Arabidopsis form a monophyletic gene family related to animal receptor kinases

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Recombinant brassinosteroid insensitive 1 receptor-like kinase autophosphorylates on serine and threonine residues and phosphorylates a conserved peptide motif in vitro

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29 September 2017

Brassinosteroid-insensitive-1 is a ubiquitously expressed leucine-rich repeat receptor serine/threonine kinase

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29 September 2017

FLS2

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29 September 2017

A Putative Leucine-Rich Repeat Receptor Kinase Involved in Brassinosteroid Signal Transduction

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Fluorescence fluctuation analysis of Arabidopsis thaliana somatic embryogenesis receptor-like kinase and brassinosteroid insensitive 1 receptor oligomerization.

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cAMP-dependent protein kinase: crystallographic insights into substrate recognition and phosphotransfer

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2 June 2018

A two-hybrid-receptor assay demonstrates heteromer formation as switch-on for plant immune receptors.

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21 January 2018

Visualization of BRI1 and BAK1(SERK3) membrane receptor heterooligomers during brassinosteroid signaling.

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21 January 2018

The Arabidopsis receptor kinase FLS2 binds flg22 and determines the specificity of flagellin perception.

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21 January 2018

A brassinosteroid-insensitive mutant in Arabidopsis thaliana exhibits multiple defects in growth and development

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21 January 2018

Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants

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21 January 2018

Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1.

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21 January 2018

HAR1 mediates systemic regulation of symbiotic organ development

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Enhancing Arabidopsis leaf growth by engineering the BRASSINOSTEROID INSENSITIVE1 receptor kinase.

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21 January 2018

BSKs are partially redundant positive regulators of brassinosteroid signaling in Arabidopsis.

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21 January 2018

Probing the Arabidopsis flagellin receptor: FLS2-FLS2 association and the contributions of specific domains to signaling function.

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21 January 2018

Structure reveals that BAK1 as a co-receptor recognizes the BRI1-bound brassinolide

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21 January 2018

BSKs mediate signal transduction from the receptor kinase BRI1 in Arabidopsis

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21 January 2018

BRI1 is a critical component of a plasma-membrane receptor for plant steroids

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21 January 2018

Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase

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21 January 2018

Autoregulation and homodimerization are involved in the activation of the plant steroid receptor BRI1.

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21 January 2018

Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling

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21 January 2018

Is kinase activity essential for biological functions of BRI1?

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21 January 2018

Tapetum determinant1 is required for cell specialization in the Arabidopsis anther

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21 January 2018

Identifiers

DOI

10.1111/TPJ.12445

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2415710

OpenCitations bibliographic resource ID

2415710

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2415710

PMC publication ID

4260089

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2415710

PubMed publication ID

24461462

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2415710

ResearchGate publication ID

259916184

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