Integrin-linked kinase

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Protein ILK PDB 2KBX.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases ILK, HEL-S-28, ILK-1, ILK-2, P59, p59integrin linked kinase
External IDs MGI: 1195267 HomoloGene: 3318 GeneCards: ILK
RNA expression pattern
PBB GE ILK 201234 at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 11: 6.6 – 6.61 Mb Chr 7: 105.74 – 105.74 Mb
PubMed search [1] [2]
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Integrin-linked kinase (ILK) is a 59kDa protein originally identified while conducting a yeast-two hybrid screen with integrin β1 as the bait protein (Hannigan et al., 1996). Since its discovery, ILK has been associated with multiple cellular functions including cell migration, cell proliferation, cell-adhesions, and signal transduction.


Transduction of extracellular matrix signals through integrins influences intracellular and extracellular functions, and appears to require interaction of integrin cytoplasmic domains with cellular proteins. Integrin-linked kinase (ILK), interacts with the cytoplasmic domain of beta-1 integrin. This gene was initially described to encode a serine/threonine protein kinase with 4 ankyrin-like repeats, which associates with the cytoplasmic domain of beta integrins and acts as a proximal receptor kinase regulating integrin-mediated signal transduction. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene.[3] Recent results showed that ILK contains 5 ankyrin-like repeats, and that the C-terminal kinase domain is actually a pseudo-kinase with adaptor function.[4][5][6]

In 2008, ILK was found to localize to the centrosome and regulate mitotic spindle organization.[7]


Integrin-linked kinase has been shown to interact with:


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ "Entrez Gene: ILK integrin-linked kinase". 
  4. ^ Lange A, Wickström SA, Jakobson M, Zent R, Sainio K, Fässler R (October 2009). "Integrin-linked kinase is an adaptor with essential functions during mouse development.". Nature. 461: 1002–6. doi:10.1038/nature08468. PMID 19829382. 
  5. ^ Fukuda K, Gupta S, Chen K, Wu C, Qin J (December 2009). "The pseudoactive site of ILK is essential for its binding to alpha-Parvin and localization to focal adhesions". Mol Cell. 36: 819–30. doi:10.1016/j.molcel.2009.11.028. PMC 2796127Freely accessible. PMID 20005845. 
  6. ^ Qin J, Wu C (October 2012). "ILK: a pseudokinase in the center stage of cell-matrix adhesion and signaling". Curr Opin Cell Biol. 24: 607–13. doi:10.1016/ PMC 3467332Freely accessible. PMID 22763012. 
  7. ^ Fielding AB, Dobreva I, McDonald PC, Foster LJ, Dedhar S (Feb 2008). "Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization". The Journal of Cell Biology. 180 (4): 681–9. doi:10.1083/jcb.200710074. PMC 2265580Freely accessible. PMID 18283114. 
  8. ^ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3: 89. doi:10.1038/msb4100134. PMC 1847948Freely accessible. PMID 17353931. 
  9. ^ Barry FA, Gibbins JM (Apr 2002). "Protein kinase B is regulated in platelets by the collagen receptor glycoprotein VI". The Journal of Biological Chemistry. 277 (15): 12874–8. doi:10.1074/jbc.M200482200. PMID 11825911. 
  10. ^ Delcommenne M, Tan C, Gray V, Rue L, Woodgett J, Dedhar S (Sep 1998). "Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase". Proceedings of the National Academy of Sciences of the United States of America. 95 (19): 11211–6. doi:10.1073/pnas.95.19.11211. PMC 21621Freely accessible. PMID 9736715. 
  11. ^ Persad S, Attwell S, Gray V, Mawji N, Deng JT, Leung D, Yan J, Sanghera J, Walsh MP, Dedhar S (Jul 2001). "Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343". The Journal of Biological Chemistry. 276 (29): 27462–9. doi:10.1074/jbc.M102940200. PMID 11313365. 
  12. ^ Leung-Hagesteijn C, Mahendra A, Naruszewicz I, Hannigan GE (May 2001). "Modulation of integrin signal transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1". The EMBO Journal. 20 (9): 2160–70. doi:10.1093/emboj/20.9.2160. PMC 125446Freely accessible. PMID 11331582. 
  13. ^ Tu Y, Li F, Goicoechea S, Wu C (Mar 1999). "The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells". Molecular and Cellular Biology. 19 (3): 2425–34. doi:10.1128/mcb.19.3.2425. PMC 84035Freely accessible. PMID 10022929. 
  14. ^ Zhang Y, Chen K, Guo L, Wu C (Oct 2002). "Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration". The Journal of Biological Chemistry. 277 (41): 38328–38. doi:10.1074/jbc.M205576200. PMID 12167643. 

Further reading[edit]