Lysophosphatidic acid differentially regulates axonal mRNA translation through 5'UTR elements Academic Article uri icon

Overview

MeSH Major

  • 5' Untranslated Regions
  • Axons
  • Calreticulin
  • Lysophospholipids

abstract

  • 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 Ca(2+) 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 eIF2α. In contrast to calreticulin, these signaling events do not activate axonal translation through β-actin's 5'UTR. Together, these data indicate that stimulation of ER stress can regulate specificity of localized mRNA translation through 5'UTR elements.

publication date

  • June 2012

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC4610731

Digital Object Identifier (DOI)

  • 10.1016/j.mcn.2012.04.001

PubMed ID

  • 22522146

Additional Document Info

start page

  • 136

end page

  • 46

volume

  • 50

number

  • 2