DORN1

Last updated
L-type lectin-domain containing receptor kinase I.9
Identifiers
Organism Arabidopsis thaliana
SymbolLECRK19
Alt. symbolsDORN1, LecRK-I.9
Entrez 836152
RefSeq (Prot) NP_001078773.1
UniProt Q9LSR8
Other data
Chromosome 5: 24.26 - 24.27 Mb

DORN1 refers to a purinergic receptor found in green plants, which is involved in extracellular ATP detection. [1] Through the process of signal transduction, DORN1 couples extracellular ATP binding (which occurs during cellular stress) to downstream signalling and ultimately gene expression, which is thought to aid in plant survival. [1] [2]

Contents

Molecular properties

In contrast to animal purinergic receptors (which are G protein-coupled receptors), DORN1 is a lectin receptor kinase (LecRK), [2] and is part of the L type lectin receptor kinases, due to its legume-like extracellular domain. [3]

In green plants such as Arabidopsis thaliana , several mutants lacking the DORN1 receptors are unable to phosphorylate mitogen-activated protein kinases after ATP stimulation. [4]

Function

DORN1 receptors may play a role in mediating wound-induced inflammatory responses in green plants, with ATP acting as a damage-associated molecular pattern molecule. In response to cell lysis, ATP is discharged and binds onto the extracellular lectin domain of the DORN1 receptor. The intracellular DORN1 kinase domain is subsequently activated, resulting in several cellular responses such as mitogen-activated protein kinase activation, increased cytosolic calcium concentration and reactive oxygen species (ROS) production, ultimately leading to the induction of defence gene expression. [2] [5]

See also

Related Research Articles

Signal transduction cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell

Signal transduction is the process by which a chemical or physical signal is transmitted through a cell as a series of molecular events, most commonly protein phosphorylation catalyzed by protein kinases, which ultimately results in a cellular response. Proteins responsible for detecting stimuli are generally termed receptors, although in some cases the term sensor is used. The changes elicited by ligand binding in a receptor give rise to a biochemical cascade, which is a chain of biochemical events known as a signaling pathway.

Calmodulin group of calcium sensors and calcium signal modulators

Calmodulin (CaM) (an abbreviation for calcium-modulated protein) is a multifunctional intermediate calcium-binding messenger protein expressed in all eukaryotic cells. It is an intracellular target of the secondary messenger Ca2+, and the binding of Ca2+ is required for the activation of calmodulin. Once bound to Ca2+, calmodulin acts as part of a calcium signal transduction pathway by modifying its interactions with various target proteins such as kinases or phosphatases.

A biochemical cascade, also known as a signaling cascade or signaling pathway, is a series of chemical reactions that occur within a biological cell when initiated by a stimulus. This stimulus, known as a first messenger, acts on a receptor that is transduced to the cell interior through second messengers which amplify the signal and transfer it to effector molecules, causing the cell to respond to the initial stimulus. Most biochemical cascades are series of events, in which one event triggers the next, in a linear fashion. At each step of the signaling cascade, various controlling factors are involved to regulate cellular actions, in order to respond effectively to cues about their changing internal and external environments.

Pattern recognition receptors (PRRs) play a crucial role in the proper function of the innate immune system. PRRs are germline-encoded host sensors, which detect molecules typical for the pathogens. They are proteins expressed, mainly, by cells of the innate immune system, such as dendritic cells, macrophages, monocytes, neutrophils and epithelial cells, to identify two classes of molecules: pathogen-associated molecular patterns (PAMPs), which are associated with microbial pathogens, and damage-associated molecular patterns (DAMPs), which are associated with components of host's cells that are released during cell damage or death. They are also called primitive pattern recognition receptors because they evolved before other parts of the immune system, particularly before adaptive immunity. PRRs also mediate the initiation of antigen-specific adaptive immune response and release of inflammatory cytokines.

The MAPK/ERK pathway is a chain of proteins in the cell that communicates a signal from a receptor on the surface of the cell to the DNA in the nucleus of the cell.

Purinergic receptor Family of cell membrane receptors in almost all tissues

Purinergic receptors, also known as purinoceptors, are a family of plasma membrane molecules that are found in almost all mammalian tissues. Within the field of purinergic signalling, these receptors have been implicated in learning and memory, locomotor and feeding behavior, and sleep. More specifically, they are involved in several cellular functions, including proliferation and migration of neural stem cells, vascular reactivity, apoptosis and cytokine secretion. These functions have not been well characterized and the effect of the extracellular microenvironment on their function is also poorly understood.

In molecular biology, extracellular signal-regulated kinases (ERKs) or classical MAP kinases are widely expressed protein kinase intracellular signalling molecules that are involved in functions including the regulation of meiosis, mitosis, and postmitotic functions in differentiated cells. Many different stimuli, including growth factors, cytokines, virus infection, ligands for heterotrimeric G protein-coupled receptors, transforming agents, and carcinogens, activate the ERK pathway.

P2Y receptor subclass of purinergic P2 receptors with signaling is coupled through a G-protein signaling mechanism

P2Y receptors are a family of purinergic G protein-coupled receptors, stimulated by nucleotides such as ATP, ADP, UTP, UDP and UDP-glucose. To date, 8 P2Y receptors have been cloned in humans: P2Y1, P2Y2, P2Y4, P2Y6, P2Y11, P2Y12, P2Y13 and P2Y14.

Wall-associated kinase protein family

Wall-associated kinases (WAKs) are one of many classes of plant proteins known to serve as a medium between the extracellular matrix (ECM) and cytoplasm of cell walls. They are serine-threonine kinases that contain epidermal growth factor (EGF) repeats, a cytoplasmic kinase and are located in the cell walls. They provide a linkage between the inner and outer surroundings of cell walls. WAKs are under a group of receptor-like kinases (RLK) that are actively involved in sensory and signal transduction pathways especially in response to foreign attacks by pathogens and in cell development. On the other hand, pectins are an abundant group of complex carbohydrates present in the primary cell wall that play roles in cell growth and development, protection, plant structure and water holding capacity.

MAP2K6 protein-coding gene in the species Homo sapiens

Dual specificity mitogen-activated protein kinase kinase 6 also known as MAP kinase kinase 6 or MAPK/ERK kinase 6 is an enzyme that in humans is encoded by the MAP2K6 gene, on chromosome 17.

P2RY1 protein-coding gene in the species Homo sapiens

P2Y purinoceptor 1 is a protein that in humans is encoded by the P2RY1 gene.

PRKD3 protein-coding gene in the species Homo sapiens

Serine/threonine-protein kinase D3 (PKD3) or PKC-nu is an enzyme that in humans is encoded by the PRKD3 gene.

P2 receptor may refer to:

P2RX4 protein-coding gene in the species Homo sapiens

P2X purinoceptor 4 is a protein that in humans is encoded by the P2RX4 gene. The product of this gene belongs to the family of purinoceptors for ATP. Multiple alternatively spliced transcript variants have been identified for this gene although their full-length natures have not been determined.

MAPK6 protein-coding gene in the species Homo sapiens

Mitogen-activated protein kinase 6 is an enzyme that in humans is encoded by the MAPK6 gene.

MAPK4 protein-coding gene in the species Homo sapiens

Mitogen-activated protein kinase 4 is an enzyme that in humans is encoded by the MAPK4 gene.

Resistance genes (R-Genes) are genes in plant genomes that convey plant disease resistance against pathogens by producing R proteins. The main class of R-genes consist of a nucleotide binding domain (NB) and a leucine rich repeat (LRR) domain(s) and are often referred to as (NB-LRR) R-genes. Generally, the NB domain binds either ATP/ADP or GTP/GDP. The LRR domain is often involved in protein-protein interactions as well as ligand binding. NB-LRR R-genes can be further subdivided into toll interleukin 1 receptor (TIR-NB-LRR) and coiled-coil (CC-NB-LRR).

BRI1-associated receptor kinase 1 is an important plant protein that has diverse functions in plant development.

Purinergic signalling Signalling complex involving purine nucleosides and their receptors

Purinergic signalling is a form of extracellular signalling mediated by purine nucleotides and nucleosides such as adenosine and ATP. It involves the activation of purinergic receptors in the cell and/or in nearby cells, thereby regulating cellular functions.

Leucine-rich repeat receptor like protein kinase

Leucine-rich repeat receptor like protein kinase are plant cell membrane localized Leucine-rich repeat (LRR) receptor kinase that play critical roles in plant innate immunity. Plants have evolved intricate immunity mechanism to combat against pathogen infection by recognizing Pathogen Associated Molecular Patterns (PAMP) and endogenous Damage Associated Molecular Patterns (DAMP). PEPR 1 considered as the first known DAMP receptor of Arabidopsis.

References

  1. 1 2 Choi J, Tanaka K, Cao Y, Qi Y, Qiu J, Liang Y, Lee SY, Stacey G (January 2014). "Identification of a plant receptor for extracellular ATP". Science. 343 (6168): 290–4. doi:10.1126/science.343.6168.290. PMID   24436418. S2CID   5029928.
  2. 1 2 3 Cao Y, Tanaka K, Nguyen CT, Stacey G (August 2014). "Extracellular ATP is a central signaling molecule in plant stress responses". Current Opinion in Plant Biology. 20: 82–7. doi:10.1016/j.pbi.2014.04.009. PMID   24865948.
  3. Bouwmeester K, Govers F (2009). "Arabidopsis L-type lectin receptor kinases: phylogeny, classification, and expression profiles". Journal of Experimental Botany. 60 (15): 4383–96. doi: 10.1093/jxb/erp277 . PMID   19773388.
  4. Adler EM (March 2014). "Of ATP receptors, opioid receptors, and AKAP regulation of calcium channels". The Journal of General Physiology. 143 (3): 313–4. doi:10.1085/jgp.201411175. PMC   3933938 . PMID   24567506.
  5. Choi J, Tanaka K, Liang Y, Cao Y, Lee SY, Stacey G (November 2014). "Extracellular ATP, a danger signal, is recognized by DORN1 in Arabidopsis". The Biochemical Journal. 463 (3): 429–37. doi:10.1042/BJ20140666. PMID   25301072.