FIGURE 2 | Anatomy of the IPP complex and its binding partners.

Integrin-linked kinase (ILK) consists of three domains, N-terminal ankyrin (ANK) repeats, a plekstrin homology (PH) domain and a C-terminal kinase domain. ANK1 binds to the LIM1 domain of particularly interesting Cys-His-rich protein (PINCH) isoforms as well as to the ILK-associated phosphatase (ILKAP). The PH domain probably binds to phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P₃). The kinase domain of ILK binds to parvins, paxillin, MIG2/kindlin-2, the cytoplasmic tails of integrins, the kinase substrate AKT/PKB (protein kinase B) and the kinase phosphatidylinositol-3-kinase-dependent kinase-1 (PDK1). PINCH isoforms, which contain five LIM domains, bind to receptor tyrosine kinases (RTKs) through the Src-homology-2 (SH2)–SH3 adaptor NCK2, thereby coupling growth-factor signalling to integrin signalling. PINCH1 binds to Ras suppressor-1 (RSU1) and thymosin-4 (T4) to influence Jun N-terminal kinase (JNK) signalling and cell migration/survival, respectively. - and -parvins can bind to F-actin directly, as well as indirectly through binding to paxillin or HIC5 (-parvin only) or -actinin (-parvin only). -Parvin also binds to the Ser/Thr kinase testicular protein kinase-1 (TESK1), whereas -parvin binds to the guanine nucleotide-exchange factor -PIX, which influences actin remodelling through the GTPases Rac and Cdc42. Interactions with integrins and the cytoskeleton also occur through a MIG2/kindlin-2–migfilin–filamin complex.

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