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Chambers, Melissa

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Chambers

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Melissa

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Chambers, Melissa

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2016 - 20182

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Author's Publications: search.filters.isAuthorOfPublication.7606261b-fcb1-4daf-81d2-86224cc24de0

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    CATCHR and HOPS-CORVET tethering complexes share a similar architecture
    (2016) Chou, Hui-Ting; Dukovski, Danijela; Chambers, Melissa; Reinisch, Karin M.; Walz, Thomas
    We show that the Saccharomyces cerevisiae GARP complex and the Cog1-4 subcomplex of the COG complex, both members of the complexes associated with tethering containing helical rods (CATCHR) family of multisubunit tethering complexes, share the same subunit organization. We also show that the HOPS complex, a tethering complex acting in the endolysosomal pathway, shares a similar architecture, suggesting that multisubunit tethering complexes use related structural frameworks.
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    A loop region of BAFF controls B cell survival and regulates recognition by different inhibitors
    (Nature Publishing Group UK, 2018) Vigolo, Michele; Chambers, Melissa; Willen, Laure; Chevalley, Dehlia; Maskos, Klaus; Lammens, Alfred; Tardivel, Aubry; Das, Dolon; Kowalczyk-Quintas, Christine; Schuepbach-Mallepell, Sonia; Smulski, Cristian R.; Eslami, Mahya; Rolink, Antonius; Hummler, Edith; Samy, Eileen; Fomekong Nanfack, Yves; Mackay, Fabienne; Liao, Maofu; Hess, Henry; Jiang, Xuliang; Schneider, Pascal
    The B cell survival factor (TNFSF13B/BAFF) is often elevated in autoimmune diseases and is targeted in the clinic for the treatment of systemic lupus erythematosus. BAFF contains a loop region designated the flap, which is dispensable for receptor binding. Here we show that the flap of BAFF has two functions. In addition to facilitating the formation of a highly active BAFF 60-mer as shown previously, it also converts binding of BAFF to TNFRSF13C (BAFFR) into a signaling event via oligomerization of individual BAFF-BAFFR complexes. Binding and activation of BAFFR can therefore be targeted independently to inhibit or activate the function of BAFF. Moreover, structural analyses suggest that the flap of BAFF 60-mer temporarily prevents binding of an anti-BAFF antibody (belimumab) but not of a decoy receptor (atacicept). The observed differences in profiles of BAFF inhibition may confer distinct biological and clinical efficacies to these therapeutically relevant inhibitors.