Activation of the retroviral budding factor ALIX |
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Authors: | Zhai Qianting Landesman Michael B Chung Hyo-Young Dierkers Adam Jeffries Cy M Trewhella Jill Hill Christopher P Sundquist Wesley I |
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Affiliation: | Department of Biochemistry, University of Utah School of Medicine, 15 N. Medical Drive East, Salt Lake City, UT 84112-5650, USA. |
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Abstract: | The cellular ALIX protein functions within the ESCRT pathway to facilitate intralumenal endosomal vesicle formation, the abscission stage of cytokinesis, and enveloped virus budding. Here, we report that the C-terminal proline-rich region (PRR) of ALIX folds back against the upstream domains and auto-inhibits V domain binding to viral late domains. Mutations designed to destabilize the closed conformation of the V domain opened the V domain, increased ALIX membrane association, and enhanced virus budding. These observations support a model in which ALIX activation requires dissociation of the autoinhibitory PRR and opening of the V domain arms. |
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