Sandbox 154: Difference between revisions
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Elongation of F-actin branches leads to the phenomenon of pushing of the plasma membrane forward in lamellopodial and filopodial extension<ref name="Chen"/>. This process relies on the dynamic equlibrium state in which G- and F-actin exist, as it is the continual polymerization of actin units on the leading edge that propels the membrane extension. Without the enzymatic ATPase function of F-actin, this process would not be possible. | Elongation of F-actin branches leads to the phenomenon of pushing of the plasma membrane forward in lamellopodial and filopodial extension<ref name="Chen"/>. This process relies on the dynamic equlibrium state in which G- and F-actin exist, as it is the continual polymerization of actin units on the leading edge that propels the membrane extension. Without the enzymatic ATPase function of F-actin, this process would not be possible. | ||
==== Actin-Myosin ==== | ==== [http://en.wikipedia.org/wiki/Actin#Actomyosin_filaments Actin-Myosin] ==== | ||
The relatively flatter shape of F-actin as compared to G-actin allows myosin to preferentially bind F-actin over G-actin. This means that F-actin, not G-actin, is the functional form of actin. It composes a large part of the thin filaments in conjunction with mysoin to give muscle contractions<ref name="Holmes2"/><ref name="Holmes3>PMID:14508495</ref>. The structure of F-actin gives it large resistance to extensive forces, such as those experienced in muscle contraction<ref name="Mitchinson"/>. | The relatively flatter shape of F-actin as compared to G-actin allows myosin to preferentially bind F-actin over G-actin. This means that F-actin, not G-actin, is the functional form of actin. It composes a large part of the thin filaments in conjunction with mysoin to give muscle contractions<ref name="Holmes2"/><ref name="Holmes3>PMID:14508495</ref>. The structure of F-actin gives it large resistance to extensive forces, such as those experienced in muscle contraction<ref name="Mitchinson"/>. | ||
