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 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>.The interactions determine the localization of the protein, its function.

Phosphorylation of conserved residues and binding to PIP2 and protein partners, is necessary for full activation of ERM proteins <ref>PMID:14993232</ref>.The interactions determine the localization of the protein, its function.

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? )

Merlin shares certain properties with the ERM family : they both have a subcellular localization to cortical action structures and both bind to the integral membrane hyaluronic acid receptor CD44.

However Merlin-1 has some properties not shared with ERM proteins.

Sandbox Reserved 705: Difference between revisions

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@@ Line 20: / Line 20: @@
 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.
-Phosphorylation and binding to PIP2 and protein partners, is necessary for full activation of ERM proteins <ref>PMID:14993232</ref>.The interactions determine the localization of the protein, its function.
+Phosphorylation of conserved residues and binding to PIP2 and protein partners, is necessary for full activation of ERM proteins <ref>PMID:14993232</ref>.The interactions determine the localization of the protein, its function.
-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? )
+Merlin shares certain properties with the ERM family : they both have a subcellular localization to cortical action structures and both bind to the integral membrane hyaluronic acid receptor CD44.
 However Merlin-1 has some properties not shared with ERM proteins.