Inositol 1,4,5,-tris-phosphate receptor

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The Inositol 1,4,5,-trisphosphate receptor, often abbreviated to 'InsP<sub>3</sub>R' or 'IP<sub>3</sub>R' is a key integral membrane [[Protein|protein]] [[Ion_channels|ion channel]] responsible for the release of [[Calcium|Ca<sup>2+</sup>]] [[Ions|ions]] from both the [[Endoplasmic Reticulum|Endoplasmic]] and [[Sarcoplasmic reticulum|Sacroplasmic Reticulum]], into the [[Cell|cell]] [[Cytosol|cytosol]]. As the name suggests, it is triggered by the binding of [[Ip3|IP<sub>3</sub> (Inositol 1,4,5,-tris-phosphate),&nbsp;in]]&nbsp;the presence of Ca<sup>2+</sup>.&nbsp;  
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The Inositol 1,4,5,-trisphosphate receptor, often abbreviated to 'InsP<sub>3</sub>R' or 'IP<sub>3</sub>R' is a key integral membrane [[Protein|protein]] [[Ion channels|ion channel]] responsible for the release of [[Calcium|Ca<sup>2+</sup>]] [[Ions|ions]] from both the [[Endoplasmic Reticulum|Endoplasmic]] and [[Sarcoplasmic_Reticulum|Sarcoplasmic Reticulum]], into the [[Cell|cell]] [[Cytosol|cytosol]]. As the name suggests, it is triggered by the binding of [[Ip3|IP<sub>3</sub> (Inositol 1,4,5,-tris-phosphate),&nbsp;in]]&nbsp;the presence of Ca<sup>2+</sup>.&nbsp;  
  
 
In order for the channel to open, [[ATP|ATP]]&nbsp;must be present at the ATP&nbsp;binding site. Note, the ATP is not hydrolised as an energy source&nbsp;by the IP<sub>3</sub>R, it merely requires ATP&nbsp;as a binding ligand for activation.&nbsp;  
 
In order for the channel to open, [[ATP|ATP]]&nbsp;must be present at the ATP&nbsp;binding site. Note, the ATP is not hydrolised as an energy source&nbsp;by the IP<sub>3</sub>R, it merely requires ATP&nbsp;as a binding ligand for activation.&nbsp;  
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IP<sub>3</sub>R is a key protein in many fundamental biological processes such as [[Apoptosis|cell death]], [[Insulin|insulin]] regulation and [[Platelets|platelet]] activation, to name a few&nbsp;<ref>http://www.uniprot.org/uniprot/Q14643</ref>. It is fundamental in generating global Ca<sup>2+</sup>&nbsp;waves via [[Calcium Induced Calcium Release|Calcium Induced Calcium Release]] (CICR), as well as elemental (puffs) and fundamental [[Calcium|calcium]] signals.  
 
IP<sub>3</sub>R is a key protein in many fundamental biological processes such as [[Apoptosis|cell death]], [[Insulin|insulin]] regulation and [[Platelets|platelet]] activation, to name a few&nbsp;<ref>http://www.uniprot.org/uniprot/Q14643</ref>. It is fundamental in generating global Ca<sup>2+</sup>&nbsp;waves via [[Calcium Induced Calcium Release|Calcium Induced Calcium Release]] (CICR), as well as elemental (puffs) and fundamental [[Calcium|calcium]] signals.  
  
In terms of structure, the IP<sub>3</sub>R (type 1) consists of 4 subunits of&nbsp;2758 amino acids&nbsp;and adopts a Homotetramer formation&nbsp;<ref>http://www.uniprot.org/uniprot/Q14643</ref>.<br>  
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In terms of structure, the IP<sub>3</sub>R (type 1) consists of 4 subunits of&nbsp;2758 [[Amino_acid|amino acids]]&nbsp;and adopts a Homotetramer formation&nbsp;<ref>http://www.uniprot.org/uniprot/Q14643</ref>.<br>  
  
 
=== References  ===
 
=== References  ===
  
 
<references />
 
<references />

Latest revision as of 12:31, 27 November 2017

The Inositol 1,4,5,-trisphosphate receptor, often abbreviated to 'InsP3R' or 'IP3R' is a key integral membrane protein ion channel responsible for the release of Ca2+ ions from both the Endoplasmic and Sarcoplasmic Reticulum, into the cell cytosol. As the name suggests, it is triggered by the binding of IP3 (Inositol 1,4,5,-tris-phosphate), in the presence of Ca2+

In order for the channel to open, ATP must be present at the ATP binding site. Note, the ATP is not hydrolised as an energy source by the IP3R, it merely requires ATP as a binding ligand for activation. 

IP3R is a key protein in many fundamental biological processes such as cell death, insulin regulation and platelet activation, to name a few [1]. It is fundamental in generating global Ca2+ waves via Calcium Induced Calcium Release (CICR), as well as elemental (puffs) and fundamental calcium signals.

In terms of structure, the IP3R (type 1) consists of 4 subunits of 2758 amino acids and adopts a Homotetramer formation [2].

References

  1. http://www.uniprot.org/uniprot/Q14643
  2. http://www.uniprot.org/uniprot/Q14643
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