Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/161717
Title: A myristoyl binding site in the SH3 domain modulates c-Src membrane anchoring
Author: Le Roux, Anabel-Lise
Mohammad, Irrem-Laareb
Mateos, Borja
Arbesú Andrés, Miguel
Gairí Tahull, Margarida
Ali Khan, Farman
Teixeira, Joao M. C.
Pons Vallès, Miquel
Keywords: Virus oncogènics
Membranes lipídiques
Lípids
Proteïnes
Oncogenic viruses
Lipid membranes
Lipids
Proteins
Issue Date: 12-Feb-2019
Publisher: Elsevier
Abstract: The c-Src oncogene is anchored to the cytoplasmic membrane through its N-terminal myristoylated SH4 domain. This domain is part of an intramolecular fuzzy complex with the SH3 and Unique domains. Here we show that the N-terminal myristoyl group binds to the SH3 domain in the proximity of the RT loop, when Src is not anchored to a lipid membrane. Residues in the so-called Unique Lipid Binding Region modulate this interaction. In the presence of lipids, the myristoyl group is released from the SH3 domain and inserts into the lipid membrane. The fuzzy complex with the SH4 and Unique domains is retained in the membrane-bound form, placing the SH3 domain close to the membrane surface and restricting its orientation. The apparent affinity of myristoylated proteins containing the SH4, Unique, and SH3 domains is modulated by these intramolecular interactions, suggesting a mechanism linking c-Src activation and membrane anchoring.
Note: Reproducció del document publicat a: https://doi.org/10.1016/j.isci.2019.01.010
It is part of: iScience, 2019, vol. 12, p. 194-203
URI: http://hdl.handle.net/2445/161717
Related resource: https://doi.org/10.1016/j.isci.2019.01.010
ISSN: 2589-0042
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

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