Structural insights into the role of the Smoothened cysteine-rich domain in Hedgehog signalling

Rajashree Rana, Candace E. Carroll, Ho-Jin Lee, Ju Bao, Suresh Marada, Christy R.R. Grace, Cristina D. Guibao, Stacey K. Ogden () and Jie J. Zheng ()
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Rajashree Rana: St Jude Children’s Research Hospital
Candace E. Carroll: St Jude Children’s Research Hospital
Ho-Jin Lee: St Jude Children’s Research Hospital
Ju Bao: St Jude Children’s Research Hospital
Suresh Marada: St Jude Children’s Research Hospital
Christy R.R. Grace: St Jude Children’s Research Hospital
Cristina D. Guibao: St Jude Children’s Research Hospital
Stacey K. Ogden: Integrated Program in Biomedical Sciences, University of Tennessee Health Science Center
Jie J. Zheng: St Jude Children’s Research Hospital

Nature Communications, 2013, vol. 4, issue 1, 1-9

Abstract: Abstract Smoothened (Smo) is a member of the Frizzled (FzD) class of G-protein-coupled receptors (GPCRs), and functions as the key transducer in the Hedgehog (Hh) signalling pathway. Smo has an extracellular cysteine-rich domain (CRD), indispensable for its function and downstream Hh signalling. Despite its essential role, the functional contribution of the CRD to Smo signalling has not been clearly elucidated. However, given that the FzD CRD binds to the endogenous Wnt ligand, it has been proposed that the Smo CRD may bind its own endogenous ligand. Here we present the NMR solution structure of the Drosophila Smo CRD, and describe interactions between the glucocorticoid budesonide (Bud) and the Smo CRDs from both Drosophila and human. Our results highlight a function of the Smo CRD, demonstrating its role in binding to small-molecule modulators.

Date: 2013
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DOI: 10.1038/ncomms3965

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