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Functional importance of localized ribosomal protein translation

Thursday, November 07, 2013 — Poster Session II

12:00 p.m. – 2:00 p.m.

FAES Academic Center (Upper-Level Terrace)




  • S. F. Clatterbuck Soper
  • S. Mili


Localization of translating mRNAs to specific subcellular domains serves a variety of important functions, such as allowing for efficient production of proteins at the point of need, reducing need for transport of individual protein molecules, allowing cells to respond more rapidly to changes in the environment, or producing a functionally distinct protein pool. Surprisingly, several screens identifying localized mRNAs have revealed that numerous ribosomal protein (r-protein) mRNAs are enriched in protrusive areas of migrating fibroblasts and in growth cones of neurons. Synthesis of r-proteins in the periphery of the cell seems counter-intuitive, as the canonical function of r-proteins, their assembly into ribosomes, occurs in the nucleolus. One clue to the role of localized r-protein translation may lie in recent reports supporting the existence of functional heterogeneity among mammalian ribosomes. Using methodologies to distinguish locally synthesized r-proteins in combination with mass spectrometry analysis we explore the possibility that r-proteins translated locally may be differentially modified compared to r-proteins produced from non-localized mRNAs. We speculate that differentially modified r-proteins are recruited into specialized ribosomes, modulating the function of the translation apparatus, and thus providing a novel mechanism for post-transcriptional regulation and for coordinating cell migration with gene expression events.

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