Molecular conformation of the full-length tumor suppressor NF2/Merlin--a small-angle neutron scattering study.

ABSTRACT: The tumor suppressor protein Merlin inhibits cell proliferation upon establishing cell-cell contacts. Because Merlin has high level of sequence similarity to the Ezrin-Radixin-Moesin family of proteins, the structural model of Ezrin-Radixin-Moesin protein autoinhibition and cycling between closed/resting and open/active conformational states is often employed to explain Merlin function. However, recent biochemical studies suggest alternative molecular models of Merlin function. Here, we have determined the low-resolution molecular structure and binding activity of Merlin and a Merlin(S518D) mutant that mimics the inactivating phosphorylation at S518 using small-angle neutron scattering and binding experiments. Small-angle neutron scattering shows that, in solution, both Merlin and Merlin(S

SUBMITTER: Ali Khajeh J 

PROVIDER: S-EPMC4407695 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature