Abstract
Signal-peptide-mediated ER localization of mRNAs encoding for membrane and secreted proteins, and RNA-zipcode-mediated intracellular targeting of mRNAs encoding for cytosolic proteins are two well-known mechanisms for mRNA localization. Here, we report a previously unidentified mechanism by which mRNA encoding for Dia1, a cytosolic protein without the signal peptide, is localized to the perinuclear ER in an RNA-zipcode-independent manner in fibroblasts. Dia1 mRNA localization is also independent of the actin and microtubule cytoskeleton but requires translation and the association of Dia1 nascent peptide with the ribosome-mRNA complex. Sequence mapping suggests that interactions of the GTPase binding domain of Dia1 peptide with active Rho are important for Dia1 mRNA localization. This mechanism can override the β-actin RNA zipcode and redirect β-actin mRNA to the perinuclear region, providing a new way to manipulate intracellular mRNA localization.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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3' Untranslated Regions
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Actins / genetics
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Actins / metabolism
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Adaptor Proteins, Signal Transducing / chemistry
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Adaptor Proteins, Signal Transducing / genetics*
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Adaptor Proteins, Signal Transducing / metabolism
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Animals
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Biological Transport
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Cells, Cultured
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Chick Embryo
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Chickens
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Endoplasmic Reticulum / genetics
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Endoplasmic Reticulum / metabolism*
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Fibroblasts / metabolism
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Formins
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Guanosine Triphosphate / metabolism*
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Humans
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Microfilament Proteins / chemistry
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Microfilament Proteins / genetics*
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Microfilament Proteins / metabolism
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Nuclear Envelope / genetics
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Nuclear Envelope / metabolism*
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Protein Binding
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Protein Transport
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RNA, Messenger / chemistry*
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RNA, Messenger / genetics
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RNA, Messenger / metabolism*
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rhoA GTP-Binding Protein / genetics
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rhoA GTP-Binding Protein / metabolism*
Substances
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3' Untranslated Regions
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Actins
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Adaptor Proteins, Signal Transducing
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DIAPH1 protein, human
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Formins
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Microfilament Proteins
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RNA, Messenger
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Guanosine Triphosphate
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rhoA GTP-Binding Protein