Stretch-activated ion channel
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Stretch-activated_ion_channel"
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Stretch-activated or stretch-gated ion channels are ion channels which open their pores in response to mechanical deformation of a neuron's plasma membrane.

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Contents

Mechanism

Though little is known about these channels, they may be linked to molecules in the cytoskeleton, which may open them by transmitting physical forces of stretch or pressure to the channels, causing them to undergo a conformational change.[1] The channels may also be pulled open due to tension on the membrane itself.[1] Opening the channels allows ions to which they are permeable to flow down their electrochemical gradients into or out of the cell, causing a change in membrane potential.

This can also be referred to as the Stress-activated gate because the gate (protein receptor) responds to pressure or stress.

Functions

Such channels are of use in the initial formation of an action potential from a mechanical stimulus, for example by the mechanoreceptors in an animal's vibrissae (whiskers).

A possible role in myoblast development has been described.[2]

Example

An example is "MID-1" (also known as "MCLC" or CLCC1.)[3][4]

See also

References

  1. ^ a b Kandel ER, Schwartz JH, Jessell TM. Principles of Neural Science, 4th ed., Pages 113-114. McGraw-Hill, New York (2000). ISBN 0-8385-7701-6
  2. ^ Formigli L, Meacci E, Sassoli C, et al (May 2007). "Cytoskeleton/stretch-activated ion channel interaction regulates myogenic differentiation of skeletal myoblasts". J. Cell. Physiol. 211 (2): 296–306. doi:10.1002/jcp.20936. PMID 17295211. 
  3. ^ Nagasawa M, Kanzaki M, Iino Y, Morishita Y, Kojima I (2001). "Identification of a novel chloride channel expressed in the endoplasmic reticulum, golgi apparatus, and nucleus". J. Biol. Chem. 276 (23): 20413–8. doi:10.1074/jbc.M100366200. PMID 11279057. 
  4. ^ Ozeki-Miyawaki C, Moriya Y, Tatsumi H, Iida H, Sokabe M (2005). "Identification of functional domains of Mid1, a stretch-activated channel component, necessary for localization to the plasma membrane and Ca2+ permeation". Exp. Cell Res. 311 (1): 84–95. doi:10.1016/j.yexcr.2005.08.014. PMID 16202999. 


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