- 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. Stretch-activated channels were first observed in chick skeletal muscles by Falguni Guharay and Frederick Sachs in 1983 and the results were published in 1984.[1] Since then strech-activated channels have been found in cells from bacteria to human as well as plants.
Contents
Mechanism
One of the three main types of ionotropic receptors or channel-linked receptor, which open by transmitting physical forces of stretch or pressure to the channels, causing them to undergo a conformational change to allow ions to pass through.[2] The channels may also be pulled open due to tension on the membrane itself.[2] 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.[3]
Example
An example is "MID-1" (also known as "MCLC" or CLCC1.)[4][5]
See also
- Mechanosensitive ion channel
- Large-conductance mechanosensitive channel
- Voltage-gated ion channels
- Ligand-gated ion channels
References
- ^ . PMC 1193237. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1193237.
- ^ 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
- ^ 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.
- ^ 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): 20413–20418. doi:10.1074/jbc.M100366200. PMID 11279057.
- ^ 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.
Ca2+: Calcium channel Ligand-gatedNa+: Sodium channel Constitutively activeProton gatedK+: Potassium channel Kvα1-6 (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8) · (2.1, 2.2) · (3.1, 3.2, 3.3, 3.4) · (4.1, 4.2, 4.3) · (5.1) · (6.1, 6.2, 6.3, 6.4)
Kvα7-12 (7.1, 7.2, 7.3, 7.4, 7.5) · (8.1, 8.2) · (9.1, 9.2, 9.3) · (10.1, 10.2) · (11.1/hERG, 11.2, 11.3) · (12.1, 12.2, 12.3)
Kvβ (1, 2, 3) · KCNIP (1, 2, 3, 4) · minK/ISK · minK/ISK-like · MiRP (1, 2, 3) · Shaker geneOther Cl-: Chloride channelHVCN1Generalsee also disorders
B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othrCategories:- Ion channels
- Cell biology stubs
- Neuroscience stubs
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