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.
Mesh Terms:
3' Untranslated Regions, Actins, Animals, Cell Line, Cerebral Cortex, Cytoplasmic Granules, Gene Expression Regulation, Humans, Intracellular Signaling Peptides and Proteins, Kinesin, Mice, Neurites, Neurons, Protein Binding, Protein Biosynthesis, Protein Transport, Protein-Serine-Threonine Kinases, RNA, RNA Transport, RNA, Messenger, Ribonucleoproteins, Tissue Extracts
Mol Cell Biol
Date: Feb. 01, 2009
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