Ceman lab in Cell Reports: How FMRP interacts with RNA helicase MOV10 to regulate translation

Ceman lab1

Binding correlation experiments of FMRP and MOV10 at active MRE sites (left) indicate that these proteins interact to suppress or increase expression of co-bound mRNAs (right).

The Ceman laboratory, with lead authors Phil Kenny and Miri Kim, have shown that FMRP is able to facilitate or suppress the translation of a subset of its target mRNAs by its interaction with the RNA helicase MOV10.

The Fragile X Mental Retardation Protein (FMRP), encoded by the FMR1 gene, is a key factor in establishing normal intelligence during brain development. FMRP is known to regulate localized protein synthesis in neurons, necessary for maintaining synaptic plasticity and dynamics at dendritic spines. Fragile X Syndrome, the clinical consequence of a loss of FMRP function, is the leading cause of inherited intellectual disability.

FMRP is an RNA binding protein, binding approximately 4% of all mRNA in the brain. However, how FMRP acts to regulate these mRNAs is poorly understood.

A study led by Dr. Stephanie Ceman has identified a protein, MOV10, which interacts with FMRP to facilitate or hinder the accessibility of the RNA Induced Silencing Complex (RISC), a complex necessary for microRNA-mediated translational regulation. The researchers findings reveal that the expression of bound mRNA can be increased or decreased depending upon FMRP’s spatial interaction with MOV10, elucidating a novel mechanism that could lead to a target in future therapeutics.

Read the full article here.

Posted June 25, 2015.