Sandbox Reserved 705: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 19: | Line 19: | ||
[[Image:imagevraie.gif |thumb|center|650px|Domain organization of ERM<ref name="utile" />]] | [[Image:imagevraie.gif |thumb|center|650px|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. | ||
'''Le domain FERM ne lie pas l'hélicale alpha? la head c pa le domaine FERM? Ce serait plus simple et il faudrai le citer pour que ça ait du sens''' | |||
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 of a C-terminal threonine by Rho kinase and binding to phosphatidylinositol 4,5-bisphosphate and protein partners, is necessary for full activation of ERM proteins <ref>PMID:14993232</ref>. They disrupt the head to tail interactions. The phosphorylations and/binding(s) determine the cellular localization and the cellular function of each specific ERM protein. | Phosphorylation of a C-terminal threonine by Rho kinase and binding to phosphatidylinositol 4,5-bisphosphate and protein partners, is necessary for full activation of ERM proteins <ref>PMID:14993232</ref>. They disrupt the head to tail interactions. The phosphorylations and/binding(s) determine the cellular localization and the cellular function of each specific ERM protein. | ||
| Line 33: | Line 34: | ||
===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 name= "utile2" />. | 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" />. | ||
The closed complex of the Merlin proteins corresponds to the tumor suppressor-active form. As the N terminus FERM domain and C terminus are maintained associated, Merlin is a closed conformation and is able to promote nuclear translocation and inhibt growth<ref>PMID:22482125</ref>. | The closed complex of the Merlin proteins corresponds to the tumor suppressor-active form. As the N-terminus FERM domain and C-terminus are maintained associated, Merlin is in a closed conformation and is able to promote nuclear translocation and inhibt growth<ref>PMID:22482125</ref>. | ||
More precisly,binding of the tail provokes dimerization and unfurling of the F2 motif of the FERM domain.The “closed” complex of merlin-1 is in fact an “open” dimer <ref name="utile" />. Ser-10 and Ser-518 phosphorylation by protein kinase A (PKA) and/or p21-activated kinase(PAK) trigger the "closed" complex <ref>PMID:18071304</ref>. | More precisly,binding of the tail provokes dimerization and unfurling of the F2 motif of the FERM domain.The “closed” complex of merlin-1 is in fact an “open” dimer <ref name="utile" />. Ser-10 and Ser-518 phosphorylation by protein kinase A (PKA) and/or p21-activated kinase(PAK) trigger the "closed" complex <ref>PMID:18071304</ref>. Phosphorylation by PAK and PKA at Ser 518 renders the protein inactive. | ||
'''Revoir et compléter la dimérisation''' | |||
===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. | ||
| Line 45: | Line 44: | ||
<scene name='Sandbox_Reserved_705/Global/4'>charged</scene> | <scene name='Sandbox_Reserved_705/Global/4'>charged</scene> | ||
<scene name='Sandbox_Reserved_705/Sheet/3'>hydrophobic,polar</scene> | <scene name='Sandbox_Reserved_705/Sheet/3'>hydrophobic,polar</scene> | ||
{{Template:ColorKey_Hydrophobic}} repartition {{Template:ColorKey_Polar}} Savoir si on montre les hydrophobes etc et leur intérêt...puisqu'on a leur répartition. Faire un schéma pour la structural difference de merlin et ERM protein pour montrer que c'est plus court. Décrire CD44 role''' | {{Template:ColorKey_Hydrophobic}} repartition {{Template:ColorKey_Polar}} Savoir si on montre les hydrophobes etc et leur intérêt...puisqu'on a leur répartition. Faire un schéma pour la structural difference de merlin et ERM protein pour montrer que c'est plus court. Décrire CD44 role. Qu'ajouter de plus? As tu des idées de schémas que l'on peut faire ou imiter à partir d'une publi ou je sais pas? As tu des idées de structure 3D que l'on peut montrer? Peux tu me dire s'il y a des fautes dans le texte en anglais ( ce qui est le cas je le sais^^)''' | ||
