Mnk is a negative regulator of cap-dependent translation in Aplysia neurons

Journal of Neurochemistry
Gabriel RossWayne S Sossin

Abstract

To investigate the mechanisms underlying regulation of eukaryotic initiation factor 4E (eIF4E) phosphorylation in Aplysia neurons, we have cloned the Aplysia homolog of the vertebrate eIF4E kinases, Mnk1 and -2. Aplysia Mnk shares many conserved regions with vertebrate Mnk, including putative eukaryotic initiation factor 4G binding regions, activation loop phosphorylation sites, and a carboxy-terminal anchoring site for MAP kinases. As expected, purified Aplysia Mnk phosphorylated Aplysia eIF4E at a conserved carboxy-terminal serine and over-expression of Aplysia Mnk in sensory neurons led to increased phosphorylation of endogenous eIF4E. Over-expression of Aplysia Mnk led to strong decreases in cap-dependent translation, while generally sparing internal ribosomal entry site (IRES)-dependent translation. However, decreases in cap-dependent translation seen after expression of Aplysia Mnk could only be partly explained by increases in eIF4E phosphorylation. In Aplysia sensory neurons, phosphorylation of eIF4E is reduced during intermediate memory formation. However, we found that this physiological regulation of eIF4E phosphorylation was independent of changes in Aplysia Mnk phosphorylation. We propose that changes in eIF4E phos...Continue Reading

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Citations

Mar 5, 2011·Microbiology and Molecular Biology Reviews : MMBR·Marie Cargnello, Philippe P Roux
Jun 30, 2012·Comparative and Functional Genomics·Gritta TettweilerGreco Hernández
May 3, 2011·Marine Biotechnology·Mathilde van der MerweRouvay Roodt-Wilding
Oct 2, 2007·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·Carol A ChrestensenThomas W Sturgill
Jan 17, 2009·Neuron·Mauro Costa-MattioliNahum Sonenberg
Nov 30, 2006·The Journal of Biological Chemistry·Carol A ChrestensenThomas W Sturgill
Nov 21, 2009·Trends in Biochemical Sciences·Greco HernándezPaul Lasko

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