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
Identifiers
Symbols ILK ; HEL-S-28; ILK-1; ILK-2; P59; p59ILK
External IDs OMIM602366 MGI1195267 HomoloGene3318 ChEMBL: 5247 GeneCards: ILK Gene
EC number 2.7.11.1
RNA expression pattern
PBB GE ILK 201234 at tn.png
More reference expression data
Orthologs
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:
6.6 – 6.61 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.

Function

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]

Interactions

Integrin-linked kinase has been shown to interact with:

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References

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Further reading

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