IGF1: Difference between revisions

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=== Stimulating interaction : IGF-1 - IGF-1R ===
=== Stimulating interaction : IGF-1 - IGF-1R ===


'''Insulin-like Growth Factor 1 Receptor''' ('''IGF-1R''') is a transmembrane protein receptor. It is composed of two α subunits and two tyrosine β subunits. Both α subunits are '''cysteine-rich region''' and therefore linked with a '''disulfide bond'''. Ligand-binding on α subunit induces activation of β subunit by autophosphorylation. It further leads to activation of the Akt and mTor pathways inside the cell. <ref>http://www.exobiologie.info/diabete/10%20recepteur.pdf, 27/01/2016</ref>
'''Insulin-like Growth Factor 1 Receptor''' ('''IGF-1R''') is a transmembrane protein receptor. It is composed of two α subunits and two tyrosine β subunits. Both α subunits are <scene name='75/751772/Igf1r/2'>cystein-rich region</scene> and therefore linked with a '''disulfide bond'''. Ligand-binding on α subunit induces activation of β subunit by autophosphorylation. It further leads to activation of the Akt and mTor pathways inside the cell. <ref>http://www.exobiologie.info/diabete/10%20recepteur.pdf, 27/01/2016</ref>


[[Image:Interactions_IGF_refait.PNG | 300 px |left]]
[[Image:Interactions_IGF_refait.PNG | 300 px |left]]
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Therefore, the various concentration of the insulin proteins regulates the cell activity in different context, for instance in excess of glucose or lack of Growth Hormone.
Therefore, the various concentration of the insulin proteins regulates the cell activity in different context, for instance in excess of glucose or lack of Growth Hormone.


Recent research demonstrated that the homology between IGF-1R and the '''insulin receptor''' (IR) subunits allow them to bind and form a functionnal hybrid IR/IGF-1R receptor.
Recent research demonstrated that the homology between IGF-1R and the '''insulin receptor''' (IR) subunits allow them to bind and form a functionnal hybrid IR/IGF-1R receptor. The exact residues interacting with one another are not known accuraretly but the docking mechanism is the same as for IGFBP.




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Maxime Julliot, Virginie Nakad, Alexia Kindler, Michal Harel, Alexander Berchansky