期刊
JOURNAL OF CELL SCIENCE
卷 124, 期 4, 页码 589-599出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.072421
关键词
Formin; Diaphanous; Translation; GTPase; Cytoskeleton; FRET; Actin
类别
资金
- NIH [R01GM070560]
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 beta-actin RNA zipcode and redirect beta-actin mRNA to the perinuclear region, providing a new way to manipulate intracellular mRNA localization.
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