Actin filament associated protein (AFAP-110) interacts directly with actin filaments through its C-terminal actin-binding domain. AFAP-110 contains additional protein-binding domains as well, and serves as an adaptor protein. By linking signaling molecules to actin filaments, AFAP-110 provides a platform for the preparation of larger signaling complexes, activates Src kinases in response to cellular signals and also directly affects Actin organization as an Actin filament cross-linking protein. AFAP-1L2 (Actin filament-associated protein 1-like 2), also known as XB130, is a 818 amino acid cytoplasmic protein that contains two Pleckstrin homology (PH) domains, which are normally found in proteins involved in intracellular signaling. Like its relative AFAP110, AFAP-1L2 interacts with Src kinase and may play a role in Src-regulated transcription activation. AFAP-1L2 is expressed in thyroid and spleen and can also be detected at lower levels in lung, brain, pancreas and kidney. There are four isoforms of AFAP-1L2 that are produced as a result of alternative splicing events.