Stretch-activated ion channel

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]

Mechanically gated ion channels are also found in the stereocilia of the inner ear. Sound waves are able to bend the stereocilia and open up ion channels leading to the creation of nerve impulses.[4]

These channels also play a role in sensing vibration and pressure via activation of Pacinian corpuscles in the skin.[5]

Example

An example is "MID-1" (also known as "MCLC" or CLCC1.)[6][7]

Other examples include, TREK-1 and TRAAK which are found in mammalian neurons and are classified as potassium channels in the tandem pore domain class.[8][9]

See also

References

  1. ^ . PMC 1193237. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1193237. 
  2. ^ 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
  3. ^ 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. 
  4. ^ Zhao, Y.; Yamoah, E. N.; Gillespie, P. G. (1996). "Regeneration of broken tip links and restoration of mechanical transduction in hair cells". Proceedings of the National Academy of Sciences of the United States of America 93 (26): 15469–15474. PMC 26428. PMID 8986835. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=26428.  edit
  5. ^ Bell, J.; Bolanowski, S.; Holmes, M. H. (1994). "The structure and function of Pacinian corpuscles: A review". Progress in neurobiology 42 (1): 79–128. PMID 7480788.  edit
  6. ^ 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. 
  7. ^ 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. 
  8. ^ Maingret, F.; Fosset, M.; Lesage, F.; Lazdunski, M.; Honoré, E. (1999). "TRAAK is a mammalian neuronal mechano-gated K+ channel". The Journal of biological chemistry 274 (3): 1381–1387. PMID 9880510.  edit
  9. ^ Patel, A. J.; Honoré, E.; Maingret, F.; Lesage, F.; Fink, M.; Duprat, F.; Lazdunski, M. (1998). "A mammalian two pore domain mechano-gated S-like K+ channel". The EMBO Journal 17 (15): 4283–4290. doi:10.1093/emboj/17.15.4283. PMC 1170762. PMID 9687497. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170762.  edit