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Lysophosphatidic acid differentially regulates axonal mRNA translation through 5 ' UTR elements
Journal article   Open access   Peer reviewed

Lysophosphatidic acid differentially regulates axonal mRNA translation through 5 ' UTR elements

Deepika Vuppalanchi, Tanuja T. Merianda, Christopher Donnelly, Almudena Pacheco, Gervan Williams, Soonmoon Yoo, Rajiv R. Ratan, Dianna E. Willis and Jeffery L. Twiss
Molecular and cellular neuroscience, v 50(2), pp 136-146
01 Jun 2012
PMID: 22522146
url
https://europepmc.org/articles/pmc4610731View
Accepted (AM)Open Access (License Unspecified) Open

Abstract

Life Sciences & Biomedicine Neurosciences Neurosciences & Neurology Science & Technology
Sensory neurons transport a complex population of mRNAs into their axons, including many encoding ER chaperone proteins. Transport of the mRNA encoding the ER chaperone protein calreticulin is regulated through 3'UTR elements. In other cellular systems, translation of chaperone protein mRNAs can be regulated by ER stress. Here, we have asked if the translation of axonal calreticulin mRNA is regulated in a different manner than its transport into axons. Treatment with lysophosphatidic acid, which is known to trigger axon retraction and stimulate ER Ca2+ release, caused a translation-dependent increase in axonal calreticulin protein levels. RNA sequences in the 5'UTR of calreticulin confer this translational control through a mechanism that requires an inactivating phosphorylation of elF2 alpha. In contrast to calreticulin, these signaling events do not activate axonal translation through beta-actin's 5'UTR. Together, these data indicate that stimulation of ER stress can regulate specificity of localized mRNA translation through 5'UTR elements.

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Collaboration types
Domestic collaboration
Web of Science research areas
Neurosciences
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