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• W2169386966 startingPage "52" @default.
• W2169386966 abstract "The protective antigen (PA) component of anthrax toxin binds the I domain of the receptor ANTXR1. Integrin I domains convert between open and closed conformations that bind ligand with high and low affinities, respectively; this process is regulated by signaling from the cytoplasmic domains. To assess whether intracellular signals might influence the interaction between ANTXR1 and PA, we compared two splice variants of ANTXR1 that differ only in their cytoplasmic domains. We found that cells expressing ANTXR1 splice variant 1 (ANTXR1-sv1) bound markedly less PA than did cells expressing a similar level of the shorter splice variant ANTXR1-sv2. ANTXR1-sv1 but not ANTXR1-sv2 associated with the actin cytoskeleton, although disruption of the cytoskeleton did not affect binding of ANTXR-sv1 to PA. Introduction of a cytoplasmic domain missense mutation found in the related receptor ANTXR2 in a patient with juvenile hyaline fibromatosis impaired actin association and increased binding of PA to ANTXR1-sv1. These results suggest that ANTXR1 has two affinity states that may be modulated by cytoplasmic signals." @default.
• W2169386966 created "2016-06-24" @default.
• W2169386966 creator A5000633792 @default.
• W2169386966 creator A5011174764 @default.
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• W2169386966 date "2009-01-01" @default.
• W2169386966 modified "2023-10-16" @default.
• W2169386966 title "The Cytoplasmic Domain of Anthrax Toxin Receptor 1 Affects Binding of the Protective Antigen" @default.
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• W2169386966 doi "https://doi.org/10.1128/iai.01073-08" @default.
• W2169386966 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2612287" @default.
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• W2169386966 hasPublicationYear "2009" @default.
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