How Arabidopsis Receptor-Like Kinase 7 (RLK7) Manifests: Delineating Its Structure and Function

Like animals, plants customarily utilize cell surface-localized receptors to keep track of environmental stimuli, specifically by plasma membrane-associated receptor-like kinases (RLKs). In comparison to other organisms, plants own a variety of RLKs, which insinuates that ligand-receptor-facilitated...

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Main Authors: Ramen Chowdhury, M. H. M. Mubassir
Format: Article
Language:English
Published: Wiley 2022-01-01
Series:Advances in Agriculture
Online Access:http://dx.doi.org/10.1155/2022/4715110
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author Ramen Chowdhury
M. H. M. Mubassir
author_facet Ramen Chowdhury
M. H. M. Mubassir
author_sort Ramen Chowdhury
collection DOAJ
description Like animals, plants customarily utilize cell surface-localized receptors to keep track of environmental stimuli, specifically by plasma membrane-associated receptor-like kinases (RLKs). In comparison to other organisms, plants own a variety of RLKs, which insinuates that ligand-receptor-facilitated molecular mechanisms regulate an array of processes during plant development. Here, we take up Arabidopsis receptor-like kinase 7 (RLK7), which shares the archetypal structure of transmembrane receptor kinases accompanied by a receptor-like ectodomain comprising of leucine-rich repeats (LRRs) along with a functional intracellular kinase domain. Interestingly, this distinctive receptor-like kinase not only orchestrates crucial steps during plant development, including the regulation of seed longevity, dormancy, and seed germination speed, but also plays a role in oxidative stress tolerance, salt stress tolerance, and pattern-triggered immunity. This review deciphers the sequence and structure and evaluates existing knowledge of the function and expression pattern of RLK7.
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spelling doaj-art-6df8b79b1a5347eeac9233dc2079ff3d2025-08-20T03:33:54ZengWileyAdvances in Agriculture2314-75392022-01-01202210.1155/2022/4715110How Arabidopsis Receptor-Like Kinase 7 (RLK7) Manifests: Delineating Its Structure and FunctionRamen Chowdhury0M. H. M. Mubassir1Department of Mathematics and Natural SciencesDepartment of Mathematics and Natural SciencesLike animals, plants customarily utilize cell surface-localized receptors to keep track of environmental stimuli, specifically by plasma membrane-associated receptor-like kinases (RLKs). In comparison to other organisms, plants own a variety of RLKs, which insinuates that ligand-receptor-facilitated molecular mechanisms regulate an array of processes during plant development. Here, we take up Arabidopsis receptor-like kinase 7 (RLK7), which shares the archetypal structure of transmembrane receptor kinases accompanied by a receptor-like ectodomain comprising of leucine-rich repeats (LRRs) along with a functional intracellular kinase domain. Interestingly, this distinctive receptor-like kinase not only orchestrates crucial steps during plant development, including the regulation of seed longevity, dormancy, and seed germination speed, but also plays a role in oxidative stress tolerance, salt stress tolerance, and pattern-triggered immunity. This review deciphers the sequence and structure and evaluates existing knowledge of the function and expression pattern of RLK7.http://dx.doi.org/10.1155/2022/4715110
spellingShingle Ramen Chowdhury
M. H. M. Mubassir
How Arabidopsis Receptor-Like Kinase 7 (RLK7) Manifests: Delineating Its Structure and Function
Advances in Agriculture
title How Arabidopsis Receptor-Like Kinase 7 (RLK7) Manifests: Delineating Its Structure and Function
title_full How Arabidopsis Receptor-Like Kinase 7 (RLK7) Manifests: Delineating Its Structure and Function
title_fullStr How Arabidopsis Receptor-Like Kinase 7 (RLK7) Manifests: Delineating Its Structure and Function
title_full_unstemmed How Arabidopsis Receptor-Like Kinase 7 (RLK7) Manifests: Delineating Its Structure and Function
title_short How Arabidopsis Receptor-Like Kinase 7 (RLK7) Manifests: Delineating Its Structure and Function
title_sort how arabidopsis receptor like kinase 7 rlk7 manifests delineating its structure and function
url http://dx.doi.org/10.1155/2022/4715110
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