FERMT2
FERMT2 (FERM domain containing kindlin 2), also known as kindlin-2, mig-2, KIND2, UNC112B and PLEKHC1, is a scaffolding protein of the kindlin family. It supports integrin activation and links sites of extracellular matrix adhesion to the actin cytoskeleton. Browse Assay Genie's current range of FERMT2 research reagents below, or read on for the biology behind the target.
FERMT2 is a scaffolding protein that enhances integrin activation mediated by talin-1 (TLN1) and/or talin-2 (TLN2), although it activates integrins only weakly on its own. It binds membranes enriched in phosphoinositides, and both this lipid binding and its interaction with integrins are required for it to promote integrin-mediated cell adhesion to the extracellular matrix and cell spreading. FERMT2 is required for the assembly of focal adhesions, takes part in connecting adhesion sites to the actin cytoskeleton, and contributes to the orchestration of actin assembly and cell shape. It also recruits FBLIM1 to focal adhesions.
Beyond adhesion, FERMT2 plays a role in the TGFB1 and integrin signalling pathways. It stabilises active CTNNB1 (β-catenin) and contributes to the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4, placing it within Wnt signalling. NCBI Gene annotation lists phosphatidylinositol-3,4,5-trisphosphate binding, protein serine/threonine kinase binding and type I transforming growth factor beta receptor binding among its functions, and places it in cell adhesion and protein localisation to cell junctions. The protein is found in the cytoplasm, cell cortex, stress fibres, focal adhesions, lamellipodium membrane, the I band of the sarcomere, the nucleus and at the cell surface.
The FERMT2 gene belongs to the fermitin and FERM domain containing gene groups, and the protein is a member of the kindlin family alongside FERMT1 and FERMT3. Earlier names include pleckstrin homology domain containing, family C (with FERM domain) member 1 (PLEKHC1) and fermitin family homolog 2. The mouse ortholog is Fermt2. FERMT2 has been described as a biomarker of acute myeloid leukaemia.
FERMT2 enhances talin-mediated integrin activation, making it a key protein for studying how cells control adhesion to the extracellular matrix.
Required for focal adhesion assembly and cell spreading, FERMT2 links adhesion sites to actin to shape cell morphology.
FERMT2 stabilises active CTNNB1, influences TCF7L2-mediated transcription and participates in TGFB1 signalling.
FERMT2 is reported as a biomarker of acute myeloid leukaemia, supporting its study in haematological disease.
FERMT2 is a scaffolding protein that enhances talin-mediated integrin activation, promotes cell adhesion and spreading, and is required for focal adhesion assembly. It connects adhesion sites to the actin cytoskeleton and also contributes to TGFB1, integrin and Wnt signalling by stabilising active CTNNB1.
FERMT2 is also called kindlin-2, mig-2, KIND2, UNC112B and PLEKHC1. Previous names include fermitin family homolog 2 and pleckstrin homology domain containing, family C (with FERM domain) member 1. Its full HGNC name is FERM domain containing kindlin 2.
FERMT2 belongs to the kindlin family, which also includes FERMT1 and FERMT3. An ortholog, Fermt2, is present in mouse. FERMT2 has also been reported as a biomarker of acute myeloid leukaemia. Check the datasheet of any product for its validated reactivity.
Other kindlin family members that share the FERM domain architecture and regulate integrin function.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q96AC1; product specifications from Assay Genie datasheets.