Insulin receptor

INSRreceptor, insulinCD220human insulin receptor–relatedIR-A
The insulin receptor (IR) is a transmembrane receptor that is activated by insulin, IGF-I, IGF-II and belongs to the large class of tyrosine kinase receptors.wikipedia
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Insulin

insulin geneINShuman insulin
The insulin receptor (IR) is a transmembrane receptor that is activated by insulin, IGF-I, IGF-II and belongs to the large class of tyrosine kinase receptors.
This is thought to avoid downregulation of insulin receptors in target cells, and to assist the liver in extracting insulin from the blood.

Diabetes

diabetes mellitusdiabeticdiabetics
Metabolically, the insulin receptor plays a key role in the regulation of glucose homeostasis, a functional process that under degenerate conditions may result in a range of clinical manifestations including diabetes and cancer.
The defective responsiveness of body tissues to insulin is believed to involve the insulin receptor.

PTPN1

PTP1Bprotein tyrosine phosphatase 1Bprotein-tyrosine phosphatase 1B
These changes facilitate the recruitment of specific adapter proteins such as the insulin receptor substrate proteins (IRS) in addition to SH2-B (Src Homology 2 - B ), APS and protein phosphatases, such as PTP1B, eventually promoting downstream processes involving blood glucose homeostasis.
PTP1B can dephosphorylate the phosphotyrosine residues of the activated insulin receptor kinase.

Cell surface receptor

transmembrane receptorreceptorcell surface receptors
The insulin receptor (IR) is a transmembrane receptor that is activated by insulin, IGF-I, IGF-II and belongs to the large class of tyrosine kinase receptors.

Receptor tyrosine kinase

receptor tyrosine kinasestyrosine kinase receptortyrosine kinase receptors
The insulin receptor (IR) is a transmembrane receptor that is activated by insulin, IGF-I, IGF-II and belongs to the large class of tyrosine kinase receptors. The Insulin Receptor is a type of tyrosine kinase receptor, in which the binding of an agonistic ligand triggers autophosphorylation of the tyrosine residues, with each subunit phosphorylating its partner.
Most RTKs are single subunit receptors but some exist as multimeric complexes, e.g., the insulin receptor that forms disulfide linked dimers in the presence of hormone (insulin); moreover, ligand binding to the extracellular domain induces formation of receptor dimers.

Fibronectin type III domain

fibronectin type IIIFNIIIfibronectin type 3
Each isometric monomer is structurally organized into 8 distinct domains consists of; a leucine-rich repeat domain (L1, residues 1-157), a cysteine-rich region (CR, residues 158-310), an additional leucine rich repeat domain (L2, residues 311-470), three fibronectin type III domains; FnIII-1 (residues 471-595), FnIII-2 (residues 596-808) and FnIII-3 (residues 809-906).
INSR; INSRR; ITGB4; Il6ST; KAL1; KALRN; L1CAM; LEPR;

Chaetochromin

4548-G05
Chaetochromin, also known as 4548-G05, is an orally active, small-molecule, selective agonist of the insulin receptor.

Insulin-like growth factor 1

IGF-1insulin-like growth factor-1IGF1
The insulin receptor (IR) is a transmembrane receptor that is activated by insulin, IGF-I, IGF-II and belongs to the large class of tyrosine kinase receptors.
IGF-1 binds to at least two cell surface receptor tyrosine kinases: the IGF-1 receptor (IGF1R), and the insulin receptor.

Protein kinase B

AktPKBAKT inhibitor
PIP 3 acts as a secondary messenger and induces the activation of phosphatidylinositol dependent protein kinase, which then activates several other kinases – most notably protein kinase B, (PKB, also known as Akt).
In contrast, mice which do not have Akt2, but have normal Akt1, have mild growth deficiency and display a diabetic phenotype (insulin resistance), again consistent with the idea that Akt2 is more specific for the insulin receptor signaling pathway.

Donohue syndrome

Leprechaunism
A few patients with homozygous mutations in the INSR gene have been described, which causes Donohue syndrome or Leprechaunism.
Affected individuals have an insulin receptor with greatly impaired functionality.

Insulin receptor substrate

NPXpY
The addition of the phosphate groups generates a binding site for the insulin receptor substrate (IRS-1), which is subsequently activated via phosphorylation.
In addition, the insulin receptor contains a NPXY motif.

GLUT4

SLC2A4GLUT 4GLUT-4
PKB triggers the translocation of glucose transporter (GLUT4) containing vesicles to the cell membrane, via the activation of SNARE proteins, to facilitate the diffusion of glucose into the cell.
In this case, insulin binds to the insulin receptor in its dimeric form and activates the receptor's tyrosine-kinase domain.

Autophosphorylation

autophosphorylateautophosphorylatedautophoshorylation
The Insulin Receptor is a type of tyrosine kinase receptor, in which the binding of an agonistic ligand triggers autophosphorylation of the tyrosine residues, with each subunit phosphorylating its partner.
Another example is the binding of insulin to insulin receptors.

Rabson–Mendenhall syndrome

Rabson-Mendenhall syndrome
Other mutations of the same gene cause the less severe Rabson-Mendenhall syndrome, in which patients have characteristically abnormal teeth, hypertrophic gingiva (gums), and enlargement of the pineal gland.
Researchers have determined that the Rabson–Mendenhall syndrome is caused by mutations of the insulin receptor gene.

GRB10

grb10 adaptor proteinGRB10'' gene
This gene encodes a growth factor receptor-binding protein that interacts with insulin receptors and insulin-like growth-factor receptors (e.g., IGF1R and IGF2R).

IRS1

IRS-1insulin receptor substrate 1insulin receptor substrate-1
IRS-1 integrates signalling from insulin receptor (InsR), insulin-like growth factor-1 receptor (IGF1R) and many other cytokine receptors and is elevated in β-catenin induced cells.

Ectonucleotide pyrophosphatase/phosphodiesterase 1

ENPP1Ectonucleotide pyrophosphatase/phosphodiesterase
Ectonucleotide pyrophosphatase/phosphodiesterase 1 has been shown to interact with Insulin receptor.

Insulin-like growth factor 2

IGF2IGF-IIIGF-2
The insulin receptor (IR) is a transmembrane receptor that is activated by insulin, IGF-I, IGF-II and belongs to the large class of tyrosine kinase receptors.

Blood sugar regulation

glucose homeostasisblood glucose regulationblood sugar control
Metabolically, the insulin receptor plays a key role in the regulation of glucose homeostasis, a functional process that under degenerate conditions may result in a range of clinical manifestations including diabetes and cancer.

Cancer

cancersmalignanciescancerous
Metabolically, the insulin receptor plays a key role in the regulation of glucose homeostasis, a functional process that under degenerate conditions may result in a range of clinical manifestations including diabetes and cancer.

Gene

genesnumber of genesgene sequence
Biochemically, the insulin receptor is encoded by a single gene, from which alternate splicing during transcription results in either IR-A or IR-B isoforms.