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Integrin-linked kinase
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. 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.〔(【引用サイトリンク】url=http://www.ncbi.nlm.nih.gov/pubmed/19829382 )〕〔(【引用サイトリンク】url=http://www.ncbi.nlm.nih.gov/pubmed/20005845 )〕〔(【引用サイトリンク】url=http://www.ncbi.nlm.nih.gov/pubmed/22763012 )〕
In 2008, ILK was found to localize to the centrosome and regulate mitotic spindle organization.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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