Sandbox Reserved 705: Difference between revisions

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The acitivity of ERM proteins is caused by the association of different regions within the protein.
The acitivity of ERM proteins is caused by the association of different regions within the protein.
The ERM proteins are regulated by changing from a closed conformation to an open, active state. This is due to intramolecular head–tail interactions,and also to interactions between their head and α-helical domains<ref name="utile2">PMID:22012890</ref>.Conformational changes modify the intramolecular contacts, allowing these proteins to bind to their partners.
The ERM proteins are regulated by changing from a closed conformation to an open, active state. This is due to intramolecular head–tail interactions,and also to interactions between their head and α-helical domains<ref name="utile2">PMID:22012890</ref>.Conformational changes modify the intramolecular contacts, allowing these proteins to bind to their partners.
Phosphorylation and binding to PIP2 and protein partners, is necessary for full activation of ERM proteins <ref>PMID:14993232</ref>.


On en parle ici de tout ce qui sera activation? : For instance Ser-10 and Ser-518 phosphorylation by PKA and/or PAK, PIP2 binding and phosphorylation of conserved threonine residues in the ERM C-terminal actin-binding site necessary for their localization to AJs ( ce que je vois pas du coup c'est comme merlin n'a pas ce domaine comment il est ammené vers sa cible? )
On en parle ici de tout ce qui sera activation? : For instance Ser-10 and Ser-518 phosphorylation by PKA and/or PAK, PIP2 binding and phosphorylation of conserved threonine residues in the ERM C-terminal actin-binding site necessary for their localization to AJs ( ce que je vois pas du coup c'est comme merlin n'a pas ce domaine comment il est ammené vers sa cible? )