Your browser doesn't support javascript.
loading
Multiple ligand binding sites regulate the Hedgehog signal transducer Smoothened in vertebrates.
Byrne, Eamon Fx; Luchetti, Giovanni; Rohatgi, Rajat; Siebold, Christian.
Afiliación
  • Byrne EF; Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.
  • Luchetti G; Departments of Biochemistry and Medicine, Stanford University School of Medicine, Stanford, CA, United States.
  • Rohatgi R; Departments of Biochemistry and Medicine, Stanford University School of Medicine, Stanford, CA, United States. Electronic address: rrohatgi@stanford.edu.
  • Siebold C; Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK. Electronic address: christian@strubi.ox.ac.uk.
Curr Opin Cell Biol ; 51: 81-88, 2018 04.
Article en En | MEDLINE | ID: mdl-29268141
The Hedgehog (Hh) pathway plays a central role in the development of multicellular organisms, guiding cell differentiation, proliferation and survival. While many components of the vertebrate pathway were discovered two decades ago, the mechanism by which the Hh signal is transmitted across the plasma membrane remains mysterious. This fundamental task in signalling is carried out by Smoothened (SMO), a human oncoprotein and validated cancer drug target that is a member of the G-protein coupled receptor protein family. Recent structural and functional studies have advanced our mechanistic understanding of SMO activation, revealing its unique regulation by two separable but allosterically-linked ligand-binding sites. Unexpectedly, these studies have nominated cellular cholesterol as having an instructive role in SMO signalling.
Asunto(s)
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Vertebrados / Proteínas de Drosophila / Proteínas Hedgehog Límite: Animals / Humans Idioma: En Revista: Curr Opin Cell Biol Año: 2018 Tipo del documento: Article Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Vertebrados / Proteínas de Drosophila / Proteínas Hedgehog Límite: Animals / Humans Idioma: En Revista: Curr Opin Cell Biol Año: 2018 Tipo del documento: Article Pais de publicación: Reino Unido