Sandbox 154: Difference between revisions

Line 47:

==== Cytoskeleton ====

F-actin is the most abundant component of the cytoskeleton of eukaryotes. It provides large amounts of tensile strength, considering its thin size. In cases where the flexibility is not desirable as a strucutral component, crosslinkages can be formed between F-actin polymers to give greater stiffness and support<ref name="Mitchinson">.

F-actin is the most abundant component of the cytoskeleton of eukaryotes. It provides large amounts of tensile strength, considering its thin size. In cases where the flexibility is not desirable as a strucutral component, crosslinkages can be formed between F-actin polymers to give greater stiffness and support<ref name="Mitchinson"/>.

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 ====

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 is the functional form of actin composing a large part of the thin filaments that function in muscle contraction<ref name="Holmes"2><ref name="Holmes3>PMID:14508495</ref>. Additionally, 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 is the functional form of actin composing a large part of the thin filaments that function in muscle contraction<ref name="Holmes"2/><ref name="Holmes3>PMID:14508495</ref>. Additionally, the structure of F-actin gives it large resistance to extensive forces, such as those experienced in muscle contraction<ref name="Mitchinson"/>.

==References==

Sandbox 154: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 47: / Line 47: @@
 ==== Cytoskeleton ====
-F-actin is the most abundant component of the cytoskeleton of eukaryotes. It provides large amounts of tensile strength, considering its thin size. In cases where the flexibility is not desirable as a strucutral component, crosslinkages can be formed between F-actin polymers to give greater stiffness and support<ref name="Mitchinson">.
+F-actin is the most abundant component of the cytoskeleton of eukaryotes. It provides large amounts of tensile strength, considering its thin size. In cases where the flexibility is not desirable as a strucutral component, crosslinkages can be formed between F-actin polymers to give greater stiffness and support<ref name="Mitchinson"/>.
-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 ====
-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 is the functional form of actin composing a large part of the thin filaments that function in muscle contraction<ref name="Holmes"2><ref name="Holmes3>PMID:14508495</ref>. Additionally, 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 is the functional form of actin composing a large part of the thin filaments that function in muscle contraction<ref name="Holmes"2/><ref name="Holmes3>PMID:14508495</ref>. Additionally, the structure of F-actin gives it large resistance to extensive forces, such as those experienced in muscle contraction<ref name="Mitchinson"/>.
 ==References==