4.4 Review

Local protein synthesis in neuronal axons: why and how we study

Journal

BMB REPORTS
Volume 48, Issue 3, Pages 139-146

Publisher

KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
DOI: 10.5483/BMBRep.2015.48.3.010

Keywords

Axon; Axon-TRAP; BONCAT; Boyden chamber; Campenot chamber; Compartmentalized culture; Laser capture microdissection; Local mRNA translation; Microfluidic device; Neuron; Protein synthesis; Puromycin tagging; Ribosome; SILAC

Funding

  1. Basic Science Research Program [NRF-2013R1A1A1009625]
  2. Bio & Medical Technology Development Program through NRF by the Korean government (MSIP) [NRF-2014M3A9 B4043638]
  3. National Research Foundation of Korea [2013R1A1A1009625] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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Adaptive brain function and synaptic plasticity rely on dynamic regulation of local proteome. One way for the neuron to introduce new proteins to the axon terminal is to transport those from the cell body, which had long been thought as the only source of axonal proteins. Another way, which is the topic of this review, is synthesizing proteins on site by local mRNA translation. Recent evidence indicates that the axon stores a reservoir of translationally silent mRNAs and regulates their expression solely by translational control. Different stimuli to axons, such as guidance cues, growth factors, and nerve injury, promote translation of selective mRNAs, a process required for the axon's ability to respond to these cues. One of the critical questions in the field of axonal protein synthesis is how mRNA-specific local translation is regulated by extracellular cues. Here, we review current experimental techniques that can be used to answer this question. Furthermore, we discuss how new technologies can help us understand what biological processes are regulated by axonal protein synthesis in vivo.

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