Protein kinase KIS localizes to RNA granules and enhances local translation.


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 beta-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.

DOI: 10.1128/MCB.01180-08

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@article{Cambray2009ProteinKK, title={Protein kinase KIS localizes to RNA granules and enhances local translation.}, author={Seraf{\'i} Cambray and Neus Pedraza and Marta Rafel and Eloi Gar{\'i} and Mart{\'i} Aldea and Carme Gallego}, journal={Molecular and cellular biology}, year={2009}, volume={29 3}, pages={726-35} }