LIM and SH3 domain protein 1 (LASP1) (LASP1)

LIM and SH3 domain protein 1 (LASP1) is a structural cytoskeletal protein that plays a critical role in cell organization and migration by binding to F-actin (UniProt Q14847) [1]. Originally identified in breast cancer metastases, LASP1 is characterized by an N-terminal LIM domain and a C-terminal SH3 domain, which facilitate its interaction with various signaling and structural proteins (NCBI Gene: 3927) [2]. In many human malignancies, including breast, gastric, and liver cancers, LASP1 is significantly overexpressed and serves as a driver of tumor cell proliferation, invasion, and epithelial-mesenchymal transition (EMT) (PubMed: 24608501) [3]. Targeting LASP1 mRNA using RNA interference (RNAi) technologies, such as siRNAs or microRNA mimics (e.g., miR-203), has demonstrated significant potential in preclinical studies to suppress oncogenic signaling and reduce metastatic spread (PubMed: 23536000) [4]. While no LASP1-specific drugs are currently FDA-approved, it remains a high-interest target for developing precision oncology treatments aimed at inhibiting cancer cell motility and improving patient outcomes in metastatic disease [5].

Other names

MLN50LASP-1LIM and SH3 domain protein 1

RNA interference (RNAi) leading to mRNA degradation or translational inhibition of the LASP1 transcript