Leucine-rich repeat and immunoglobulin domain-containing protein-1 (Lrig1) negative regulatory action toward ErbB receptor tyrosine kinases is opposed by leucine-rich repeat and immunoglobulin domain-containing protein 3 (Lrig3)

Hanine Rafidi; Francisco Mercado; Michael Astudillo; William H.D. Fry; Matthew Saldana; Kermit L. Carraway; Colleen Sweeney

Journal ArticleOPEN ACCESS

Leucine-rich repeat and immunoglobulin domain-containing protein-1 (Lrig1) negative regulatory action toward ErbB receptor tyrosine kinases is opposed by leucine-rich repeat and immunoglobulin domain-containing protein 3 (Lrig3)

Journal of Biological Chemistry (2013) 288(30) 21593-21605

DOI: 10.1074/jbc.M113.486050

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Abstract

Background: Lrig1 is a negative regulator of oncogenic receptor tyrosine kinases. Results: Lrig3 opposes Lrig1 negative regulatory action and enhances ErbB receptor stability. Conclusion: Lrig1 and Lrig3 oppose one another. Significance: Despite structural homology, Lrig1 and Lrig3 are functionally distinct. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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Rafidi, H., Mercado, F., Astudillo, M., Fry, W. H. D., Saldana, M., Carraway, K. L., & Sweeney, C. (2013). Leucine-rich repeat and immunoglobulin domain-containing protein-1 (Lrig1) negative regulatory action toward ErbB receptor tyrosine kinases is opposed by leucine-rich repeat and immunoglobulin domain-containing protein 3 (Lrig3). Journal of Biological Chemistry, 288(30), 21593–21605. https://doi.org/10.1074/jbc.M113.486050

Leucine-rich repeat and immunoglobulin domain-containing protein-1 (Lrig1) negative regulatory action toward ErbB receptor tyrosine kinases is opposed by leucine-rich repeat and immunoglobulin domain-containing protein 3 (Lrig3)

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