Fermitin family member 1 (FERMT1) (FERMT1)

Fermitin family member 1 (FERMT1), also known as Kindlin-1, is a focal adhesion protein that plays a critical role in the activation of integrins, which are essential for cell-extracellular matrix (ECM) adhesion [UniProt: Q9BQL6]. It functions by binding to the cytoplasmic tail of beta-integrin subunits, working in tandem with talin to induce the conformational changes necessary for high-affinity ligand binding, a process known as inside-out signaling [PubMed: 19074551]. Beyond its role in adhesion, FERMT1 is involved in regulating cell migration, proliferation, and the organization of the actin cytoskeleton [NCBI Gene: 59701]. Mutations in the FERMT1 gene lead to Kindler syndrome, a rare autosomal recessive disorder characterized by skin blistering, photosensitivity, and progressive skin atrophy [PubMed: 12145234]. In oncology, FERMT1 is frequently overexpressed in various cancers, such as breast, lung, and colon cancer, where it is associated with epithelial-mesenchymal transition (EMT), increased metastatic potential, and poor patient prognosis [PubMed: 23435373]. Although there are currently no FDA-approved drugs that directly target FERMT1, it is considered a promising therapeutic target for preventing cancer metastasis and managing genetic skin disorders [PubMed: 31515456].

Other names

Kindlin-1KIND1UNC112AURB

Integrin activation through binding to the beta-integrin cytoplasmic tail, facilitating inside-out signaling and focal adhesion assembly.