ZNRF3/RNF43--A direct linkage of extracellular recognition and E3 ligase activity to modulate cell surface signalling.

Zebisch, Matthias; Jones, E Yvonne

Zebisch, Matthias; Jones, E Yvonne.

Affiliation

Zebisch M; Evotec (UK) Ltd, 114 Innovation Drive, Milton Park, Abingdon, Oxfordshire OX14 4RZ, United Kingdom.
Jones EY; Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, United Kingdom. Electronic address: yvonne@strubi.ox.ac.uk.

Prog Biophys Mol Biol ; 118(3): 112-8, 2015 Sep.

Article in En | MEDLINE | ID: mdl-25937466

Subject(s)

DNA-Binding Proteins/metabolism; Extracellular Space/metabolism; Signal Transduction; Ubiquitin-Protein Ligases/metabolism; Amino Acid Sequence; Animals; DNA-Binding Proteins/chemistry; Humans; Molecular Sequence Data; Protein Multimerization; Protein Structure, Tertiary; Ubiquitin-Protein Ligases/chemistry

Key words

LGR4/5/6; Rspondin; Transmembrane E3 RING ligase; Wnt signalling

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Signal Transduction / Ubiquitin-Protein Ligases / DNA-Binding Proteins / Extracellular Space Limits: Animals / Humans Language: En Journal: Prog Biophys Mol Biol Year: 2015 Document type: Article Affiliation country: United kingdom Country of publication: United kingdom

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