@article {3339,
	title = {NMDAR mediated dynamic changes in mA inversely correlates with neuronal translation.},
	journal = {Sci Rep},
	volume = {12},
	year = {2022},
	month = {2022 07 05},
	pages = {11317},
	abstract = {<p>Epitranscriptome modifications are crucial in translation regulation and essential for maintaining cellular homeostasis. N6 methyladenosine (mA) is one of the most abundant and well-conserved epitranscriptome modifications, which is known to play a pivotal role in diverse aspects of neuronal functions. However, the role of mA modifications with respect to activity-mediated translation regulation and synaptic plasticity has not been studied. Here, we investigated the role of mA modification in response to NMDAR stimulation. We have consistently observed that 5\&nbsp;min NMDAR stimulation causes an increase in eEF2 phosphorylation. Correspondingly, NMDAR stimulation caused a significant increase in the mA signal at 5\&nbsp;min time point, correlating with the global translation inhibition. The NMDAR induced increase in the mA signal is accompanied by the redistribution of the mA marked RNAs from translating to the non-translating pool of ribosomes. The increased mA levels are well correlated with the reduced FTO levels observed on NMDAR stimulation. Additionally, we show that inhibition of FTO prevents NMDAR mediated changes in mA levels. Overall, our results establish RNA-based molecular readout which corelates with the NMDAR-dependent translation regulation which helps in understanding changes in protein synthesis.</p>
},
	keywords = {Adenosine, Neurons, Phosphorylation, Receptors, N-Methyl-D-Aspartate, RNA},
	issn = {2045-2322},
	doi = {10.1038/s41598-022-14798-3},
	author = {Gowda, Naveen Kumar Chandappa and Nawalpuri, Bharti and Ramakrishna, Sarayu and Jhaveri, Vishwaja and Muddashetty, Ravi S}
}
@article {1744,
	title = {NMDAR mediated translation at the synapse is regulated by MOV10 and FMRP.},
	journal = {Mol Brain},
	volume = {12},
	year = {2019},
	month = {2019 Jul 10},
	pages = {65},
	abstract = {<p>Protein synthesis is crucial for maintaining synaptic plasticity and synaptic signalling. Here we have attempted to understand the role of RNA binding proteins, Fragile X Mental Retardation Protein (FMRP) and Moloney Leukemia Virus 10 (MOV10) protein in N-Methyl-D-Aspartate Receptor (NMDAR) mediated translation regulation. We show that FMRP is required for translation downstream of NMDAR stimulation and MOV10 is the key specificity factor in this process. In rat cortical synaptoneurosomes, MOV10 in association with FMRP and Argonaute 2 (AGO2) forms the inhibitory complex on a subset of NMDAR responsive mRNAs. On NMDAR stimulation, MOV10 dissociates from AGO2 and promotes the translation of its target mRNAs. FMRP is required to form MOV10-AGO2 inhibitory complex and to promote translation of MOV10 associated mRNAs. Phosphorylation of FMRP appears to be the potential switch for NMDAR mediated translation and in the absence of FMRP, the distinct translation response to NMDAR\&nbsp;stimulation is lost. Thus, FMRP and MOV10 have an important regulatory role in NMDAR mediated translation at the synapse.</p>
},
	issn = {1756-6606},
	doi = {10.1186/s13041-019-0473-0},
	author = {Kute, Preeti Madhav and Ramakrishna, Sarayu and Neelagandan, Nagammal and Chattarji, Sumantra and Muddashetty, Ravi S}
}
