PLS1
Description
The PLS1 (plastin 1) is a protein-coding gene located on chromosome 3.
Fimbrin, also known as plastin 1, is a protein encoded by the PLS1 gene in humans. It acts as an actin cross-linking protein, crucial for the formation of filopodia. Fimbrin belongs to the calponin homology (CH) domain superfamily of actin cross-linking proteins. Like other members, it features a conserved 27 kDa actin-binding domain containing a duplicated calponin-homologous sequence. Besides cross-linking actin filaments into bundles and networks, CH domains bind intermediate filaments and signaling proteins to the actin cytoskeleton. Fimbrin's cross-linking activity alters the actin structure, potentially influencing its interaction with other actin-binding proteins and contributing to cytoskeletal regulation. In humans, three highly similar fimbrin isoforms have been identified: I-, T-, and L-fimbrin. L-fimbrin, exclusively found in normal or transformed leukocytes, undergoes phosphorylation in response to factors like interleukin-1. I-fimbrin is expressed in intestinal and kidney epithelial cells, while T-fimbrin is found in epithelial and mesenchymal cells derived from solid tissues and does not become phosphorylated.
PLS1 is also known as DFNA76.
