ArticleMolecular immunology2010
Interleukin-1 Receptor-Associated Kinase-1 (IRAK-1) functionally associates with PKCepsilon and VASP in the regulation of macrophage migration.
Article in Molecular immunology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Phosphoregulation of interleukin-1 receptor-associated kinase 1 in inflammatory signaling.Frontiers in immunology · 2026Review
- Article
- Hypoxia-induced up-regulation of VASP promotes invasiveness and metastasis of hepatocellular carcinoma.Theranostics · 2018Article
- The role of 3-ketosteroid 1(2)-dehydrogenase in the pathogenicity of Mycobacterium tuberculosis.BMC microbiology · 2013Article
- Molecular mechanism responsible for the priming of macrophage activation.The Journal of biological chemistry · 2013Article
- Cholesterol oxidase is indispensable in the pathogenesis of Mycobacterium tuberculosis.PloS one · 2013Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Macrophage migration is mediated by complex cellular signaling processes and cytoskeleton re-arrangement. In particular, recent advances indicate that the innate immunity signaling process plays a key role in the regulation of macrophage migration. In this report, we have provided evidence demonstrating the involvement of a key innate immunity signaling kinase, Interleukin-1 Receptor-Associated Kinase-1 (IRAK-1) as a critical modulator of macrophage migration. Macrophage migration induced by phorbol 12-myristate 13-acetate (PMA) is significantly attenuated in IRAK-1(-/-) macrophages as compared to wild type macrophages. Mechanistically, we demonstrated that IRAK-1 works downstream of PKCepsilon and upstream of VASP, a member of Ena/VASP family proteins. IRAK-1 forms a close complex with PKCepsilon as well as VASP, and participates in PMA-induced phosphorylation of VASP. Notably, IRAK-1 contains a novel EVH1 domain binding motif (L(167)WPPPP) within its N-terminus, which is responsible for its interaction with VASP. The mutant IRAK-1 (L167A/W168A) fails to associate with VASP. Our findings provide a novel facet regarding the molecular signaling process regulating macrophage migration.
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