ArticlePlant physiology2023
BRASSINOSTEROID INSENSITIVE1 internalization can occur independent of ligand binding.
Article in Plant physiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- A mechanistic framework for the recognition of chemically diverse brassinosteroids by BRI1-family receptor kinases.Nature plants · 2026Article
- Removal of seed coat H3K27me3 in Arabidopsis requires noncanonical functions of brassinosteroid receptors.The Plant cell · 2026Article
- Brassinosteroid Signaling Dynamics: Ubiquitination-Dependent Regulation of Core Signaling Components.International journal of molecular sciences · 2025Review
- Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants.The Plant cell · 2024Review
- Influence of Exogenous 24-Epicasterone on the Hormonal Status of Soybean Plants.Plants (Basel, Switzerland) · 2023Article
- Another tool in the receptor endocytosis kit: ligand-insensitive BRASSINOSTEROID INSENSITIVE1.Plant physiology · 2023Article
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 5 countries.
Funding
Abstract
The brassinosteroid (BR) hormone and its plasma membrane (PM) receptor BR INSENSITIVE1 (BRI1) are one of the best-studied receptor-ligand pairs for understanding the interplay between receptor endocytosis and signaling in plants. BR signaling is mainly determined by the PM pool of BRI1, whereas BRI1 endocytosis ensures signal attenuation. As BRs are ubiquitously distributed in the plant, the tools available to study the BRI1 function without interference from endogenous BRs are limited. Here, we designed a BR binding-deficient Arabidopsis (Arabidopsis thaliana) mutant based on protein sequence-structure analysis and homology modeling of members of the BRI1 family. This tool allowed us to re-examine the BRI1 endocytosis and signal attenuation model. We showed that despite impaired phosphorylation and ubiquitination, BR binding-deficient BRI1 internalizes similarly to the wild type form. Our data indicate that BRI1 internalization relies on different endocytic machineries. In addition, the BR binding-deficient mutant provides opportunities to study non-canonical ligand-independent BRI1 functions.
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Registered trials
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 Socratic graph.