PI3K: Difference between revisions

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Phosphatidylinositol 3-kinase (PI3K) adds a phosphate group to the 3C position in a inosital ring in [[Phosphatidylinositol|Phosphatidylinositol]].  
<p>Phosphatidylinositol 3-kinase (PI3K)&#160;adds a phosphate group to the 3C position in a inosital ring in &lt;a href="Phosphatidylinositol"&gt;Phosphatidylinositol&lt;/a&gt;.  
 
</p><p>For example:  
For example:  
</p><p>&lt;a href="Phosphatidylinositol 4,5-bisphosphate"&gt;PI-4,5-phosphate&lt;/a&gt; (PIP<sub>2</sub>) + ATP ----&gt; PI-3,4, 5-bisphosphate (PIP<sub>3</sub>) + ADP<br />
 
</p><p>This in the context of the &lt;a href="Insulin"&gt;Insulin&lt;/a&gt;&#160;pathway allows the resulting &lt;a href="Phosphatidylinositol 4,5-bisphosphate"&gt;PIP<sub>3</sub>&lt;/a&gt; to remain bound to the plasma membrane. This initiates a signal cascade which can cause &lt;a href="Glut 4"&gt;GLUT 4&lt;/a&gt; translocation, decreased synthesis of glycerol and fatty acids, increased &lt;a href="Glycogen synthesis"&gt;glycogen synthesis&lt;/a&gt; and increased &lt;a href="Proteins"&gt;protein&lt;/a&gt; synthesis in the cell.  
[[Phosphatidylinositol 4,5-bisphosphate|PI-4,5-phosphate]] (PIP<sub>2</sub>) + ATP ----&gt; PI-3,4, 5-bisphosphate (PIP<sub>3</sub>) + ADP<br>
</p><p>The enzyme has 2 subunits:  
 
</p>
This in the context of the [[Insulin|Insulin]]&nbsp;pathway allows the resulting [[Phosphatidylinositol 4,5-bisphosphate|PIP<sub>3</sub>]] to remain bound to the plasma membrane. This initiates a signal cascade which can cause [[Glut 4|GLUT 4]] translocation, decreased synthesis of glycerol and fatty acids, increased [[Glycogen synthesis|glycogen synthesis]] and increased [[Proteins|protein]] synthesis in the cell.  
<ol><li>Regulatory subunit, p85 (85 kDa), contains 2 &lt;a href="SH2 domains"&gt;SH2 domains&lt;/a&gt; and 1 &lt;a href="SH3 domains"&gt;SH3 domain&lt;/a&gt;.  
 
</li><li>Catalytic subunit, p110 (110 kDa).
The enzyme has 2 subunits:  
</li></ol>
 
<p>The &lt;a href="SH2 domains"&gt;SH2 domain&lt;/a&gt; in the context of the &lt;a href="Insulin"&gt;Insulin&lt;/a&gt; pathway binds p85 to phosphorylated &lt;a href="Tyrosine"&gt;tyrosines&lt;/a&gt;&#160;on the &lt;a href="Insulin receptor substrate"&gt;Insulin receptor substrate&lt;/a&gt; (&lt;a href="Insulin receptor substrate"&gt;IRS&lt;/a&gt;). The &lt;a href="SH3 domains"&gt;SH3 domain&lt;/a&gt; targets the &lt;a href="Proline"&gt;proline rich&lt;/a&gt; section of p85 binding both regulatory and catalytic subunits together.  
#Regulatory subunit, p85 (85 kDa), contains 2 [[SH2 domains|SH2 domains]] and 1 [[SH3 domains|SH3 domain]].  
</p><p>&#160;  
#Catalytic subunit, p110 (110 kDa).
</p><p>There are three classes of P13K enzymes. Class I can phosphorylate 3 different substrates: non-phosphorylated phosphatidylinositol, inositol monophosphate and bisphosphate inositol. The catalytic subunit is p100 and the regulatory subunit is p85. This class of P13K are associated with being of &lt;a href="Oncogenes"&gt;oncogenic&lt;/a&gt; nature, as the catalytic subunit can become mutated, unlike class II and&#160;III.<span class="fck_mw_ref">Phosphatidylinositol 3-kinase (PI3K): The Oncoprotein Peter K. Vogt PubMed (accessed 22/10/2018) https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2955792/</span>
 
</p>
The [[SH2 domains|SH2 domain]] in the context of the [[Insulin|Insulin]] pathway binds p85 to phosphorylated [[Tyrosine|tyrosines]]&nbsp;on the [[Insulin receptor substrate|Insulin receptor substrate]] ([[Insulin receptor substrate|IRS]]). The [[SH3 domains|SH3 domain]] targets the [[Proline|proline rich]] section of p85 binding both regulatory and catalytic subunits together.  
 
&nbsp;  
 
There are three classes of P13K enzymes. Class I can phosphorylate 3 different substrates: non-phosphorylated phosphatidylinositol, inositol monophosphate and bisphosphate inositol. The catalytic subunit is p100 and the regulatory subunit is p85. This class of P13K are associated with being of [[Oncogenes|oncogenic]] nature, as the catalytic subunit can become mutated, unlike class II and&nbsp;III.<ref>Phosphatidylinositol 3-kinase (PI3K): The Oncoprotein Peter K. Vogt PubMed (accessed 22/10/2018) https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2955792/</ref>

Revision as of 14:23, 22 October 2018

Phosphatidylinositol 3-kinase (PI3K) adds a phosphate group to the 3C position in a inosital ring in <a href="Phosphatidylinositol">Phosphatidylinositol</a>.

For example:

<a href="Phosphatidylinositol 4,5-bisphosphate">PI-4,5-phosphate</a> (PIP2) + ATP ----> PI-3,4, 5-bisphosphate (PIP3) + ADP

This in the context of the <a href="Insulin">Insulin</a> pathway allows the resulting <a href="Phosphatidylinositol 4,5-bisphosphate">PIP3</a> to remain bound to the plasma membrane. This initiates a signal cascade which can cause <a href="Glut 4">GLUT 4</a> translocation, decreased synthesis of glycerol and fatty acids, increased <a href="Glycogen synthesis">glycogen synthesis</a> and increased <a href="Proteins">protein</a> synthesis in the cell.

The enzyme has 2 subunits:

  1. Regulatory subunit, p85 (85 kDa), contains 2 <a href="SH2 domains">SH2 domains</a> and 1 <a href="SH3 domains">SH3 domain</a>.
  2. Catalytic subunit, p110 (110 kDa).

The <a href="SH2 domains">SH2 domain</a> in the context of the <a href="Insulin">Insulin</a> pathway binds p85 to phosphorylated <a href="Tyrosine">tyrosines</a> on the <a href="Insulin receptor substrate">Insulin receptor substrate</a> (<a href="Insulin receptor substrate">IRS</a>). The <a href="SH3 domains">SH3 domain</a> targets the <a href="Proline">proline rich</a> section of p85 binding both regulatory and catalytic subunits together.

 

There are three classes of P13K enzymes. Class I can phosphorylate 3 different substrates: non-phosphorylated phosphatidylinositol, inositol monophosphate and bisphosphate inositol. The catalytic subunit is p100 and the regulatory subunit is p85. This class of P13K are associated with being of <a href="Oncogenes">oncogenic</a> nature, as the catalytic subunit can become mutated, unlike class II and III.Phosphatidylinositol 3-kinase (PI3K): The Oncoprotein Peter K. Vogt PubMed (accessed 22/10/2018) https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2955792/