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This is a list of actin-binding proteins in alphabetical order.
Alpha-actinin is an actin-binding protein with multiple roles in different cell types.
The prolin-rich domain interacts with cortactin and actin-binding protein 1.
Profilin as a ubiquitous actin-binding protein is associated with most actin monomers in cells.
Profilin is an actin-binding protein involved in the dynamic turnover and restructuring of the actin cytoskeleton.
Sla2p is an actin-binding protein involved in endocytosis, thus indicating HIP1 in this role.
A class of actin-binding proteins, called cross-linking proteins, dictate the formation of these structures.
Filamin is an actin-binding protein involved in cytokinesis and ring canal formation [ 38, 39].
ADF/cofilin is a family of actin-binding proteins which disassembles actin filaments.
Villin is a 92.5 kDa tissue-specific actin-binding protein associated with the actin core bundle of the brush border.
Gelsolin is an actin-binding protein that is a key regulator of actin filament assembly and disassembly.
Nebulin is an actin-binding protein which is localized to the thin filament of the sarcomeres in skeletal muscle.
Actin-binding proteins (also known as ABP) are proteins that bind to actin.
Subsequently, ADP-actin dissociates slowly from the pointed end, a process significantly accelerated by the actin-binding protein, cofilin.
Three-helix bundles often occur in actin-binding proteins and in DNA-binding proteins.
They contain actin filaments cross-linked into bundles by actin-binding proteins, e.g. fascin and fimbrin.
ADF/cofilins are small actin-binding proteins composed of a single ADF-H domain.
Actin-binding protein anillin is a protein that in humans is encoded by the ANLN gene.
This triterpene can inhibit the phosphorylation of the cofilin protein, a family of actin-binding proteins that disassembles actin filaments.
The product of this gene belongs to the actin-binding proteins ADF (Actin-Depolymerizing Factor)/cofilin family.
Many actin-binding proteins, including α-actinin, β-spectrin, dystrophin, utrophin and fimbrin, do this through the actin-binding calponin homology domain.
Members of the coronin family, such as CORO1B, are WD repeat-containing actin-binding proteins that regulate cell motility.
Adenylate Cyclase Associated Protein is an actin-binding protein that was originally identified as a binding partner for adenylate cyclase.
These structures are regulated by many other classes of actin-binding proteins, including motor proteins, branching proteins, severing proteins, polymerization promoters, and capping proteins.
Because Shroom3 is an actin-binding protein and accumulates on the apical side, the most likely mechanism is that Shroom3 aggregates the actin meshwork, generating a squeezing force.