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.

'''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 C-terminal tail domain contains an F-actin binding site in the last 30 residues. This domain interacts with the FERM domain as an extended, meandering polypeptide beginning with a β-strand associated with β5 in F3 followed by four helices, the first two of which bind lobe F2 and second two lobe F3. The FERM-tail complex represents a dormant form of the protein in which membrane protein and active binding sites are masked.<ref>http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1796844/</ref>

'''C'est ce que j'ai lu sur les ERM proteines mais après c'était l'un des points que j'avait pas trop compris All ERM proteins appear to be regulated by transitioning from a closed conformation to an open, active state following severing of intramolecular head–tail interactions, and of interactions between their head and central α-helical domains. The crystal structures of the FERM domains of ezrin and merlin,the moesin head:tail complex, and the moesin FERM domain in complex with its central α-helical domain have been solved. The moesin head:tail complex structure established that this interaction buries the charged F-actin binding site, and that the C-terminal tail covers large portions of the F2 and F3 motifs of the FERM domain. il sempblerait que la tete soit le C terminal mais je suis pas sur.'''

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.

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.
 '''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 C-terminal tail domain contains an F-actin binding site in the last 30 residues. This domain interacts with the FERM domain as an extended, meandering polypeptide beginning with a β-strand associated with β5 in F3 followed by four helices, the first two of which bind lobe F2 and second two lobe F3. The FERM-tail complex represents a dormant form of the protein in which membrane protein and active binding sites are masked.<ref>http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1796844/</ref>
+'''C'est ce que j'ai lu sur les ERM proteines mais après c'était l'un des points que j'avait pas trop compris All ERM proteins appear to be regulated by transitioning from a closed conformation to an open, active state following severing of intramolecular head–tail interactions, and of interactions between their head and central α-helical domains. The crystal structures of the FERM domains of ezrin and merlin,the moesin head:tail complex, and the moesin FERM domain in complex with its central α-helical domain have been solved. The moesin head:tail complex structure established that this interaction buries the charged F-actin binding site, and that the C-terminal tail covers large portions of the F2 and F3 motifs of the FERM domain. il sempblerait que la tete soit le C terminal mais je suis pas sur.'''
 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.