Beta4 integrin amplifies ErbB2 signaling to promote mammary tumorigenesis

Article Abstract:

The role of the signaling and cell-adhesion receptor Beta4 integrin during ErbB2-mediated tumorigenesis by introducing a targeted deletion of the Beta4 signaling domain into a mouse model of ErbB2-induced mammary carcinoma is examined. Results demonstrate that Beta4 integrin promotes tumor progression by amplifying ErbB2 signaling and identify Beta4 as a potential target for molecular therapy of breast cancer.

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In vivo beta1 integrin function requires phosphorylation-independent regulation by cytoplasmic tyrosines

Article Abstract:

Replacement of both beta1 integrin cytoplasmic tyrosines with alanines, resulting in the loss of all phosphotyrosine-binding (PTB) domain interaction, causes complete loss of beta1 integrin function in vivo. In contrast, replacement of beta1 integrin cytoplasmic tyrosine phenylalanines, a mutation that prevents tyrosine phosphorylation, conserves in vivo integrin function.

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Development requires activation but not phosphorylation of beta1 integrins

Article Abstract:

The importance of beta1 integrin cytoplasmic tyrosines after embryogenesis is assessed using elegant chimera studies. It is found that tyrosine phosphorylation may contribute to regulation of alphaIIbbeta3 and to a smaller extent alpha2beta1 in platelets, but this modification does not appear to affect the function of most beta1 integrins during development.

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