Protein Kinase KIS Localizes to RNA Granules and Enhances Local Translation

  • Cambray S
  • Pedraza N
  • Rafel M
  • et al.
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Abstract

The regulation of mRNA transport is a fundamental process for cytoplasmic sorting of transcripts and spatially controlled translational derepression once properly localized. There is growing evidence that translation is locally modulated as a result of specific synaptic inputs. However, the underlying molecular mechanisms that regulate this translational process are just emerging. We show that KIS, a serine/threonine kinase functionally related to microtubule dynamics and axon development, interacts with three proteins found in RNA granules: KIF3A, NonO, and eEF1A. KIS localizes to RNA granules and colocalizes with the KIF3A kinesin and the β-actin mRNA in cultured cortical neurons. In addition, KIS is found associated with KIF3A and 10 RNP-transported mRNAs in brain extracts. The results of knockdown experiments indicate that KIS is required for normal neurite outgrowth. More important, the kinase activity of KIS stimulates 3′ untranslated region-dependent local translation in neuritic projections. We propose that KIS is a component of the molecular device that modulates translation in RNA-transporting granules as a result of local signals. Copyright © 2009, American Society for Microbiology. All Rights Reserved.

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Cambray, S., Pedraza, N., Rafel, M., Garí, E., Aldea, M., & Gallego, C. (2009). Protein Kinase KIS Localizes to RNA Granules and Enhances Local Translation. Molecular and Cellular Biology, 29(3), 726–735. https://doi.org/10.1128/mcb.01180-08

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