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? ) | ||
