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MIM.602366 11p15.5-p15.4

Tuesday 10 May 2005

ILK is a serine-threonine protein kinase that associates with the cytoplasmic domain of beta integrins and acts as a proximal receptor kinase regulating integrin-mediated signal transduction.

Integrin-linked kinase (ILK) is a potent intracellular kinase involved in the regulation of multiple proliferation and survival kinases, including protein kinase B/Akt (AKT), glycogen synthase kinase-3β (GSK3β or GSK3B) and extracellular signal-regulated kinases 1 and 2 (ERK1/2 or ERK1).

The ternary complex of integrin-linked kinase (ILK), PINCH and parvin functions as a signalling platform for integrins by interfacing with the actin cytoskeleton and many diverse signalling pathways.

All these proteins have synergistic functions at focal adhesions. These proteins might also have separate roles within a cell. They function as regulators of gene transcription or cell-cell adhesion.


ILK is overexpressed and acts oncogenically in a wide variety of primary tumors and genetic models, resulting in induction of tumor cell proliferation, migration, adhesion and angiogenic behaviours.

ILK could have an oncogenic role in alveolar rhabdomyosarcoma (ARMS), and suggest a novel tumor-suppressive role for ILK signaling in embryonal rhabdomyosarcoma (ERMS), mediated through the non-canonical ILK target axis, JNK-c-Jun.


- Legate KR, Montanez E, Kudlacek O, Fassler R. ILK, PINCH and parvin: the tIPP of integrin signalling. Nat Rev Mol Cell Biol. 2006 Jan;7(1):20-31. PMID: 16493410

- Wu C. PINCH, N(i)ck and the ILK: network wiring at cell-matrix adhesions. Trends Cell Biol. 2005 Sep;15(9):460-6. PMID: 16084094

- Hannigan G, Troussard AA, Dedhar S. Integrin-linked kinase: a cancer therapeutic target unique among its ILK. Nat Rev Cancer. 2005 Jan;5(1):51-63. PMID: 15630415