Integrin-linked kinase

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Integrin-linked kinase
Protein ILK PDB 2KBX.png
Rendering based on PDB 2KBX.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols ILK ; HEL-S-28; ILK-1; ILK-2; P59; p59ILK
External IDs OMIM602366 MGI1195267 HomoloGene3318 IUPHAR: 2041 ChEMBL: 5247 GeneCards: ILK Gene
EC number
RNA expression pattern
PBB GE ILK 201234 at tn.png
More reference expression data
Species Human Mouse
Entrez 3611 16202
Ensembl ENSG00000166333 ENSMUSG00000030890
UniProt Q13418 O55222
RefSeq (mRNA) NM_001014794 NM_001161724
RefSeq (protein) NP_001014794 NP_001155196
Location (UCSC) Chr 11:
6.62 – 6.63 Mb
Chr 7:
105.74 – 105.74 Mb
PubMed search [1] [2]

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.[1] 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.[2][3][4]

In 2008, ILK was found to localize to the centrosome and regulate mitotic spindle organization.[5]


Integrin-linked kinase has been shown to interact with LIMS1,[6][7] AKT1,[8][9][10] ILKAP,[11] ACP6[12] and parvin.[13]


  1. ^ "Entrez Gene: ILK integrin-linked kinase". 
  2. ^ "Integrin-linked kinase is an adaptor with essential functions during mouse development.". NCBI. October 2009. 
  3. ^ "The pseudoactive site of ILK is essential for its binding to alpha-Parvin and localization to focal adhesions". NCBI. December 2009. 
  4. ^ "ILK: a pseudokinase in the center stage of cell-matrix adhesion and signaling". NCBI. October 2012. 
  5. ^ Fielding AB, Dobreva I, McDonald PC, Foster LJ, Dedhar S (February 2008). "Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization". J. Cell Biol. 180 (4): 681–9. doi:10.1083/jcb.200710074. PMC 2265580. PMID 18283114. 
  6. ^ Tu, Y; Li F; Goicoechea S; Wu C (March 1999). "The LIM-Only Protein PINCH Directly Interacts with Integrin-Linked Kinase and Is Recruited to Integrin-Rich Sites in Spreading Cells". Mol. Cell. Biol. 19 (3): 2425–34. PMC 84035. PMID 10022929. 
  7. ^ Zhang, Yongjun; Chen Ka; Guo Lida; Wu Chuanyue (October 2002). "Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration". J. Biol. Chem. 277 (41): 38328–38. doi:10.1074/jbc.M205576200. PMID 12167643. 
  8. ^ Barry, Fiona A; Gibbins Jonathan M (April 2002). "Protein kinase B is regulated in platelets by the collagen receptor glycoprotein VI". J. Biol. Chem. 277 (15): 12874–8. doi:10.1074/jbc.M200482200. PMID 11825911. 
  9. ^ Delcommenne, M; Tan C; Gray V; Rue L; Woodgett J; Dedhar S (September 1998). "Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase". Proc. Natl. Acad. Sci. U.S.A. 95 (19): 11211–6. doi:10.1073/pnas.95.19.11211. PMC 21621. PMID 9736715. 
  10. ^ Persad, S; Attwell S; Gray V; Mawji N; Deng J T; Leung D; Yan J; Sanghera J; Walsh M P; Dedhar S (July 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". J. Biol. Chem. 276 (29): 27462–9. doi:10.1074/jbc.M102940200. PMID 11313365. 
  11. ^ Leung-Hagesteijn, C; Mahendra A; Naruszewicz I; Hannigan G E (May 2001). "Modulation of integrin signal transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1". EMBO J. 20 (9): 2160–70. doi:10.1093/emboj/20.9.2160. PMC 125446. PMID 11331582. 
  12. ^ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. 
  13. ^ "A central multifunctional role of integrin-linked kinase at muscle attachment sites". NCBI. April 2011. 

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