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Figure 1


Fig. 1. The ILK interactome. ILK is localized in FAs, where it forms multiprotein complexes with several proteins that are involved in cytoskeletal dynamics and cell-signaling cascades. The N-terminal ankyrin repeats of ILK interact directly with several key proteins, including PINCH, ILKAP, SPARC and T-cadherin. PINCH also couples ILK to T 4, Rsu1 and NCK2. NCK2 associates with growth factor receptors, which potentially links ILK to growth-factor signaling. The central PH-like domain of ILK binds to PtdIns(3,4,5)P3 and is required for PI3K-dependent activation of ILK. The C-terminal kinase domain of ILK interacts with 1 and 3 integrin, as well as with several actin-binding adaptor proteins, including -parvin, -parvin, paxillin, Mig-2 and Wech. Key binding partners that are involved in cell signaling also bind the ILK kinase domain, including PDK1, Akt, Rictor and Src. In particular, a direct interaction between Rictor and ILK is important for phosphorylation of Akt at Ser473. Rsu1, Ras suppressor 1; T 4, thymosin 4; RTK, receptor tyrosine kinase; GF, growth factor; SPARC, secreted protein acidic and rich in cysteine; PIP3, PtdIns(3,4,5)P3; PDK1, protein-dependent kinase 1; N, N terminal; C, C terminal; P, phosphorylation site; ECM, extracellular matrix; SH3, Src homology 3; CH2, calponin homology 2; ANK, ankyrin repeat; Mig-2, mitogen-induced gene 2 (also known as fermitin family homolog 2); PHI-1, phosphatase holoenzyme inhibitor 1.





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