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.