Search results for IRS1

Showing 28 results out of 48

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Species

Types

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Protein (5 results from a total of 5)

Identifier: R-HSA-2425392
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: IRS1: P35568
Identifier: R-HSA-74769
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P35568
Identifier: R-HSA-198366
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: IRS1: P35568
Identifier: R-HSA-74772
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P35568
Identifier: R-HSA-2445090
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: P35568

Reaction (6 results from a total of 22)

Identifier: R-HSA-9603437
Species: Homo sapiens
Compartment: plasma membrane, cytosol
Activated wild-type NTRK3 (TRKC), as well as constitutively active ETV6-NTRK3 oncogene, a product of translocation between ETV6 and NTRK3 gene loci in congenital fibrosarcoma and cellular mesoblastic nephroma, are able to bind to adaptor protein IRS1 (Morrison et al. 2002, Lannon et al. 2004, Jin et al. 2008). Binding of IRS1 to NTRK3 is enhanced in the presence of SRC (Jin et al. 2008).
Identifier: R-HSA-198211
Species: Homo sapiens
Compartment: cytoplasmic side of plasma membrane
IRS1 and IRS2 bind directly to TRK receptors phosphorylated at Y490, through their phosphotyrosine- binding (PTB) domains.
Identifier: R-HSA-74737
Species: Homo sapiens
Compartment: cytosol
IRS1, IRS2 and IRS3 are all known to bind the regulatory subunit of PI3K via its SH2 domain, an interaction that itself activates the kinase activity of the PI3K catalytic subunit (Rivachandran et al. 2001).
Identifier: R-HSA-74747
Species: Homo sapiens
Compartment: cytosol
At the beginning of this reaction, 1 molecule of 'phospho-IRS' is present. At the end of this reaction, 1 molecule of 'Orthophosphate', and 1 molecule of 'IRS' are present.

This reaction takes place in the 'cytosol' and is mediated by the 'protein tyrosine phosphatase activity' of 'protein tyrosine phosphatase' (Pederson et al.2001).
Identifier: R-HSA-2671873
Species: Homo sapiens
Compartment: plasma membrane, cytosol
SH2B1 in the LEP:LEPR:JAK2:SH2B1 complex can bind either IRS1 or IRS2 (Duan et al. 2004, Li et al. 2007). The binding brings IRS1/2 into proximity with JAK2 for phosphorylation.
Identifier: R-HSA-74736
Species: Homo sapiens
Compartment: cytosol
Inactive p21ras:GDP is anchored to the plasma membrane by a farnesyl residue. Insulin stimulation results in phosphorylation of IRS1/2 on tyrosine residues. GRB2 binds the phosphotyrosines via its SH2 domain. As IRS is phosphorylated by the insulin receptor near to the plasma membrane, the GRB2:SOS1:IRS interaction brings SOS1 and p21 Ras into close proximity.

Set (6 results from a total of 6)

Identifier: R-HSA-112322
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-198369
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-198273
Species: Homo sapiens
Compartment: cytosol
The proteins mentioned here are examples of IRS family members acting as indicated for IRS.
Identifier: R-HSA-2445131
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-2445139
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-2428932
Species: Homo sapiens
Compartment: plasma membrane

Complex (6 results from a total of 10)

Identifier: R-HSA-198299
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-109800
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-74694
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-5686316
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-198344
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-213135
Species: Homo sapiens
Compartment: plasma membrane

Pathway (5 results from a total of 5)

Identifier: R-HSA-74713
Species: Homo sapiens
IRS is one of the mediators of insulin signalling events. It is activated by phosphorylation and triggers a cascade of events involving PI3K, SOS, RAF and the MAP kinases. The proteins mentioned under IRS are examples of IRS family members acting as indicated. More family members are to be confirmed and added in the future. Using receptor mutagenesis studies it is known that IRS1 via its PTB domain binds to the insulin receptor at the juxtamembrane region at tyrosine 972. The interaction is further stabilized by the PH domain of IRS1 which interacts with the phospholipids of the plasma membrane. This allows the receptor to phosphorylate IRS1 on up to 13 of its tyrosine residues. Once phosphorylated the IRS1 falls away from the receptor. Now in a tyrosine phosphorylated and hence activated state other proteins can interact with the IRS proteins.
Identifier: R-HSA-2428924
Species: Homo sapiens
Compartment: cytosol, plasma membrane
After autophosphorylation the type 1 insulin-like growth factor receptor (IGF1R) binds and phosphorylates scaffold proteins, IRS1/2/4 and SHC1, which in turn bind effectors possessing enzymatic activity (recently reviewed in Pavelic et al. 2007, Chitnis et al. 2008, Maki et al. 2010, Parrella et al. 2010, and Siddle et al. 2012). IRS1/2/4 can bind both PI3K (via the p85 subunit of PI3K) and the GRB2:SOS complex. PI3K activates PKB (AKT, AKT1) signaling. GRB:SOS stimulates RAS to exchange GDP for GTP leading to activation of RAF and MAPK.
Identifier: R-HSA-2428928
Species: Homo sapiens
Compartment: cytosol, plasma membrane
The phosphorylated type 1 insulin-like growth factor receptor phosphorylates IRS1, IRS2, IRS4 and possibly other IRS/DOK family members (reviewed in Pavelic et al. 2007, Chitnis et al. 2008, Maki et al. 2010, Parrella et al. 2010, Siddle et al. 2012). The phosphorylated IRS proteins serve as scaffolds that bind the effector molecules PI3K and GRB2:SOS. PI3K then activates PKB (AKT) signaling while GRB2:SOS activates RAS-RAF-MAPK signaling.
Identifier: R-HSA-9603381
Species: Homo sapiens
The PI3K complex, composed of PIK3R1 and PIK3CA, co-immunoprecipitates with NTRK3 (TRKC), activated by NTF3 (NT-3) treatment (Yuen and Mobley 1999). Activation of NTRK3 correlates with activating phosphorylation of AKT, the main mediator of PI3K signaling (Tognon et al. 2001, Jin et al. 2008), and is dependent on PI3K activity (Tognon et al. 2001). NTRK3-mediated activation of PI3K signaling depends on SRC activation and the adaptor protein IRS1, but the exact mechanism is not known (Morrison et al. 2002, Lannon et al. 2004, Jin et al. 2008).
Identifier: R-HSA-2586552
Species: Homo sapiens
Compartment: plasma membrane, cytosol
Leptin (LEP, OB, OBS), a circulating adipokine, and its receptor LEPR (DB, OBR) control food intake and energy balance and are implicated in obesity-related diseases (recently reviewed in Amitani et al. 2013, Dunmore and Brown 2013, Cottrell and Mercer 2012, La Cava 2012, Marroqui et al. 2012, Paz-Filho et al. 2012, Denver et al. 2011, Lee 2011, Marino et al. 2011, Morton and Schwartz 2011, Scherer and Buettner 2011, Shan and Yeo 2011, Wauman and Tavernier 2011, Dardeno et al. 2010, Bjorbaek 2009, Morris and Rui 2009, Myers et al. 2008), including cancer (Guo et al. 2012), inflammation (Newman and Gonzalez-Perez 2013, Iikuni et al. 2008), and angiogenesis (Gonzalez-Perez et al. 2013).
The identification of spontaneous mutations in the leptin gene (ob or LEP) and the leptin receptor gene (Ob-R, db or LEPR) genes in mice opened up a new field in obesity research. Leptin was discovered as the product of the gene affected by the ob (obesity) mutation, which causes obesity in mice. Likewise LEPR is the product of the gene affected by the db (diabetic) mutation. Leptin binding to LEPR induces canonical (JAK2/STATs; MAPK/ERK 1/2, PI-3K/AKT) and non-canonical signaling pathways (PKC, JNK, p38 MAPK and AMPK) in diverse cell types. The binding of leptin to the long isoform of LEPR (OB-Rl) initiates a phosphorylation cascade that results in transcriptional activation of target genes by STAT5 and STAT3 and activation of the PI3K pathway(not shown here), the MAPK/ERK pathway, and the mTOR/S6K pathway. Shorter LEPR isoforms with truncated intracellular domains are unable to activate the STAT pathway, but can transduce signals by way of activation of JAK2, IRS-1 or ERKs, including MAPKs.
LEPR is constitutively bound to the JAK2 kinase. Binding of LEP to LEPR causes a conformational change in LEPR that activates JAK2 autophosphorylation followed by phosphorylation of LEPR by JAK2. Phosphorylated LEPR binds STAT3, STAT5, and SHP2 which are then phosphorylated by JAK2. Phosphorylated JAK2 binds SH2B1 which then binds IRS1/2, resulting in phosphorylation of IRS1/2 by JAK2. Phosphorylated STAT3 and STAT5 dimerize and translocate to the nucleus where they activate transcription of target genes (Jovanovic et al. 2010). SHP2 activates the MAPK pathway. IRS1/2 activate the PI3K/AKT pathway which may be the activator of mTOR/S6K.
Several isoforms of LEPR have been identified (reviewed in Gorska et al. 2010). The long isoform (LEPRb, OBRb) is expressed in the hypothalamus and all types of immune cells. It is the only isoform known to fully activate signaling pathways in response to leptin. Shorter isoforms (LEPRa, LEPRc, LEPRd, and a soluble isoform LEPRe) are able to interact with JAK kinases and activate other pathways, however their roles in energy homeostasis are not fully characterized.
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