Sandbox Reserved 705: Difference between revisions
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[[Image:imageutile.gif |thumb|center|350px|Domain organization of ERM<ref name="utile" />]] | [[Image:imageutile.gif |thumb|center|350px|Domain organization of ERM<ref name="utile" />]] | ||
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. | 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>. | ||
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? ) | ||
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==Specificity of merlin FERM domain== | ==Specificity of merlin FERM domain== | ||
===Structural differences=== | ===Structural differences=== | ||
The overall architecture of merlin is similar to that of ERM proteins. Indeed they have almost the same organization : a FERM domain,a central α-helical rod, but lack a C-terminal actin-binding site<ref | The overall architecture of merlin is similar to that of ERM proteins. Indeed they have almost the same organization : a FERM domain,a central α-helical rod, but lack a C-terminal actin-binding site<ref name= "utile2" />. | ||
===CD44=== | ===CD44=== | ||
CD44 is a cell-surface receptor for hyaluronan (HA a ligand). When HA binds to CD44 the complex promotes tumorigenesis it means it promotes tumor invasion and metastasis. Indeed, CD44 is a receptor presents in the TA3 carcinome mammaire cells and Tr6BC1 schwannoma cells and HA allows their growth. | CD44 is a cell-surface receptor for hyaluronan (HA a ligand). When HA binds to CD44 the complex promotes tumorigenesis it means it promotes tumor invasion and metastasis. Indeed, CD44 is a receptor presents in the TA3 carcinome mammaire cells and Tr6BC1 schwannoma cells and HA allows their growth. | ||
