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Actin-binding proteins (also known as ABPs) are proteins that bind to actin. [1] This may mean ability to bind actin monomers, or polymers, or both. Many actin-binding proteins, including α-actinin, β-spectrin, dystrophin, utrophin and fimbrin, do this through the actin-binding calponin homology domain .
The Rho family of GTPases is a family of small (~21 kDa) signaling G proteins, and is a subfamily of the Ras superfamily.The members of the Rho GTPase family have been shown to regulate many aspects of intracellular actin dynamics, and are found in all eukaryotic kingdoms, including yeasts and some plants.
The crystallization of G-actin was possible due to the use of a rhodamine conjugate that impedes polymerization by blocking the amino acid cys-374. [1] Christine Oriol-Audit died in the same year that actin was first crystallized but she was the researcher that in 1977 first crystallized actin in the absence of Actin Binding Proteins (ABPs).
Actin-binding proteins regulate assembly and disassembly of actin filaments. [4] Cofilin, a member of the ADF/cofilin family is actually a protein with 70% sequence identity to destrin, making it part of the ADF/cofilin family of small ADP-binding proteins. [5] [6] The protein binds to actin monomers and filaments, G actin and F actin ...
In molecular biology, the cyclase-associated protein family (CAP) is a family of highly conserved actin-binding proteins present in a wide range of organisms including yeast, flies, plants, and mammals. CAPs are multifunctional proteins that contain several structural domains. CAP is involved in species-specific signalling pathways.
Filament end-tracking protein (e.g., formins, VASP, N-WASP) Filament-nucleator known as the Actin-Related Protein-2/3 (or Arp2/3) complex; Filament cross-linkers (e.g., α-actinin, fascin, and fimbrin) Actin monomer-binding proteins profilin and thymosin β4; Filament barbed-end cappers such as Capping Protein and CapG, etc.
A certain GAP and a certain G protein happen to be expressed in the same time and place, and that is how the cell ensures specificity. Meanwhile, scaffold proteins can also sequester the proper GAP to its G protein and enhance the proper binding interactions. [8] These binding interactions may be specific for a particular GAP and G protein.
[3] [4] G 12 /G 13 are not targets of pertussis toxin or cholera toxin, as are other classes of G protein alpha subunits. [5] G proteins G 12 and G 13 regulate actin cytoskeletal remodeling in cells during movement and migration, including cancer cell metastasis. [6] G 13 is also essential for receptor tyrosine kinase-induced migration of ...