Molecular mechanisms of hedgehog signal transduction by the G-protein coupled receptor smoothened

Eamon Byrne

Abstract:

The Hedgehog signalling pathway is an essential developmental pathway present in all bilaterians that is involved in embryogenesis, body patterning and stem cell homeostasis. Dysregulation of the Hh pathway leads to various kinds of cancer, such as basal cell carcinoma and medulloblastoma. Smoothened (SMO), a Frizzled-type G-protein coupled receptor (GPCR), is the essential transmembrane signal transducer within the Hh pathway, conveying the signal from the upstream transmembrane protein, ...

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APA Style

Byrne, E. (2017). Molecular mechanisms of hedgehog signal transduction by the G-protein coupled receptor smoothened [PhD thesis]. University of Oxford.

MLA Style

Byrne, Eamon. Molecular Mechanisms of Hedgehog Signal Transduction by the G-Protein Coupled Receptor Smoothened. University of Oxford, 2017.

Chicago Style

Byrne, Eamon. 2017. “Molecular Mechanisms of Hedgehog Signal Transduction by the G-Protein Coupled Receptor Smoothened.” PhD thesis, University of Oxford.
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Authors

+ Eamon Byrne More by this author

Department:

Structural Biology

Contributors

+ Christian Siebold

Department:

Structural Biology

Role:

Supervisor

Funding

+ Nuffield Department of Medicine More from this funder

Funding agency for:

Eamon Byrne

+ Clarendon trust More from this funder

Funding agency for:

Eamon Byrne

+ University College, Oxford More from this funder

Funding agency for:

Eamon Byrne

Bibliographic Details

Type of award:: DPhil
Level of award:: Doctoral
Awarding institution:: University of Oxford

Item Description

Language:: English
Keywords:: GPCR

x-ray crystallography
Subjects:: Hedgehog signalling pathway

structural biology

Smoothened

Related Items

Has part:: Structural basis of Smoothened regulation by its extracellular domains
Description:: Developmental signals of the Hedgehog (Hh) and Wnt families are transduced across the membrane by Frizzled-class G-protein-coupled receptors (GPCRs) composed of both a heptahelical transmembrane domain (TMD) and an extracellular cysteine-rich domain (CRD). How the large extracellular domains of GPCRs regulate signalling by the TMD is unknown. We present crystal structures of the Hh signal transducer and oncoprotein Smoothened, a GPCR that contains two distinct ligand-binding sites: one in its...
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License:: Terms and Conditions of Use for Oxford University Research Archive

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