LIM and SH3 domain protein 1 (LASP1)

LIM and SH3 domain protein 1 (abbreviated as LASP1) is a member of a LIM protein subfamily, defined by the presence of one N-terminal LIM domain and one C-terminal SH3 domain, with two intermediary nebulin-like repeats[1][3][5]. These structural features allow the protein to interact with a variety of cytoskeletal and signaling proteins, such as F-actin, zyxin, CXCR2, dynamin, and others[1][3]. Initially discovered as a gene overexpressed in metastatic breast cancer, LASP1 is now known to play versatile roles in cell structure, cytoskeletal dynamics, and intracellular signaling[1][3][5]. Its ability to shuttle between the cytoplasm and the nucleus enables it to regulate gene expression, participate in chromatin remodeling, and influence cell cycle progression[3]. Overexpression of LASP1 is linked to aggressive cancer phenotypes, including enhanced cell migration, invasion, and metastasis, making it a potential biomarker for cancer diagnosis and prognosis[1][3]. Currently, no approved drugs directly target LASP1, and its primary relevance is as a molecular marker and signaling mediator rather than a direct therapeutic target[1][3][5].

Other names

LASP1MLN50LIM-SH3 protein 1LASP-1

Not applicable (no direct drugs; however, LASP1 modulates signaling and cytoskeletal rearrangement)