Johnson's Monday Lab Sandbox for Insulin Receptor
From Proteopedia
(Difference between revisions)
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==Function of the Receptor== | ==Function of the Receptor== | ||
| - | The insulin receptor serves as the gateway for the regulation of various cellular processes. These processes include but are not limited to glucose transport, glycogen storage, autophagy, apoptosis, and gene expression. Additionally, the insulin receptor has been associated with the development of diseases such as Alzheimer's, Type II Diabetes, and cancer <ref name="Scapin" />. Characterization of the structure of the insulin receptor as well as understanding of the molecular mechanisms which initiate a conformational change are important for understanding the role that the insulin receptor plays within a cell and in the development of disease. | + | The insulin receptor resides within the plasma membrane of insulin target cells of different organs, such as the liver, and tissues including skeletal muscle and adipose. Activation of the insulin receptor is dependent upon insulin binding. Once activated, the receptor serves as the gateway for the regulation of various cellular processes. These processes include but are not limited to glucose transport, glycogen storage, autophagy, apoptosis, and gene expression. Additionally, the insulin receptor has been associated with the development of diseases such as Alzheimer's, Type II Diabetes, and cancer <ref name="Scapin" />. Characterization of the structure of the insulin receptor as well as understanding of the molecular mechanisms which initiate a conformational change are important for understanding the role that the insulin receptor plays within a cell and in the development of disease. |
==Insulin== | ==Insulin== | ||
WHAT IS INSULIN. WHAT DOES IT LOOK LIKE? WHERE IS IT MADE? WHAT DOES IT DO? WHERE DOES IT GO? WHY DO WE NEED IT? | WHAT IS INSULIN. WHAT DOES IT LOOK LIKE? WHERE IS IT MADE? WHAT DOES IT DO? WHERE DOES IT GO? WHY DO WE NEED IT? | ||
==Structure== | ==Structure== | ||
| - | The insulin receptor is a [http://en.wikipedia.org/wiki/Receptor_tyrosine_kinase receptor tyrosine kinase] heterotetramer which | + | The insulin receptor is a [http://en.wikipedia.org/wiki/Receptor_tyrosine_kinase receptor tyrosine kinase]. It is a heterotetramer which is constructed from two homodimers. Each homodimer maintains an extracellular domain, transmembrane helix, and an intracellular domain. The extracellular domain is divided into alpha and beta subunits. The alpha subunit is characterized by two leucine-rich regions and one cysteine rich region. The beta subunit contains three fibronectin type III domains. The alpha and beta subunits of the extracellular domains fold over one another and form a "V" shape when the insulin receptor is unactivated. Upon activation, the extracellular domain undergoes a conformational change and forms a "T" shape. |
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| + | The structure of the extracellular domain is stabilized through covalent bonds. The alpha subunits are linked through two disulfide bonds. Cysteine 435 and cysteine 524 of one alpha subunit are bound to cysteine 468 and cysteine 524 of the other alpha subunit, respectively <ref name="Schäffer" />. | ||
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| + | The insulin receptor extends intracellularly from the beta subunits of the ectodomain by way of a [http://en.wikipedia.org/wiki/Transmembrane_protein transmembrane] helix. Intracellularly, the insulin receptor contains two tyrosine kinase domains. C TERM ALPHA HELIX. COVALENT DISULFIDE BONDS | ||
===Insulin Binding=== | ===Insulin Binding=== | ||
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<ref name="Meyts"> DOI:10.1007/BF00400837</ref> | <ref name="Meyts"> DOI:10.1007/BF00400837</ref> | ||
<ref name="Scapin">DOI:10.1038/nature26153</ref> | <ref name="Scapin">DOI:10.1038/nature26153</ref> | ||
| + | <ref name="Schäffer">DOI:10.1016/0006-291X(92)92250-2</ref> | ||
<ref name="Uchikawa"> DOI:10.7554/eLife.48630</ref> | <ref name="Uchikawa"> DOI:10.7554/eLife.48630</ref> | ||
Revision as of 19:54, 23 March 2020
Insulin Receptor
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