IP3 receptor: Difference between revisions
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[[Ip3|IP3]] receptor is a receptor situated on the [[Endoplasmic_Reticulum|Endoplasmic Reticulum]] in the [[cytoplasm|cytoplasm]] of a [[cell|cell]]. It is opened by the presence of IP3 and [[calcium|calcium]] and allows calcium stored in the Endoplasmic Reticulum to be released into the cytoplasm of the cell. | |||
The IP3 receptor is essential for some key biological processes including; cell division, cell proliferation, fertilization, behaviour and learning and development. The receptor acts as a second messenger which leads to the release of calcium from its storage sites. It is also found abundantly in the Cerebellum as well as endoplasmic Reticulum. It has an asymmetrical structure consisting of a C-terminal alpha helical domain and an N-terminal Beta trefoil domain. | The IP3 receptor is essential for some key biological processes including; [[cell division|cell division]], [[cell proliferation|cell proliferation]], fertilization, behaviour and learning and development. The receptor acts as a [[Second_messengers|second messenger]] which leads to the release of calcium from its storage sites. It is also found abundantly in the [[Cerebellum|Cerebellum]] as well as endoplasmic Reticulum. It has an asymmetrical structure consisting of a [[C terminal|C-terminal]][[alpha helical domain|alpha helical domain]] and an N-terminal Beta trefoil domain. | ||
Latest revision as of 02:37, 30 October 2015
IP3 receptor is a receptor situated on the Endoplasmic Reticulum in the cytoplasm of a cell. It is opened by the presence of IP3 and calcium and allows calcium stored in the Endoplasmic Reticulum to be released into the cytoplasm of the cell.
The IP3 receptor is essential for some key biological processes including; cell division, cell proliferation, fertilization, behaviour and learning and development. The receptor acts as a second messenger which leads to the release of calcium from its storage sites. It is also found abundantly in the Cerebellum as well as endoplasmic Reticulum. It has an asymmetrical structure consisting of a C-terminalalpha helical domain and an N-terminal Beta trefoil domain.