Journal
JOURNAL OF CELL SCIENCE
Volume 118, Issue 11, Pages 2425-2433Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.02371
Keywords
actin cytoskeleton; microtubules; mRNA targeting; cell motility; myosin
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Funding
- NCI NIH HHS [P01 CA100324, CA100324] Funding Source: Medline
- NHLBI NIH HHS [T32-HL-07194, T32 HL007194] Funding Source: Medline
- NIAMS NIH HHS [AR41480, R01 AR041480] Funding Source: Medline
- NIGMS NIH HHS [R01 GM070560, GM70560] Funding Source: Medline
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The actin-related protein 2/3 (Arp2/3) complex is a crucial actin polymerization nucleator and is localized to the leading protrusions of migrating cells. However, how the multiprotein complex is targeted to the protrusions remains unknown. Here, we demonstrate that mRNAs for the seven subunits of the Arp2/3 complex are localized to the protrusions in fibroblasts, supporting a hypothesis that the Arp2/3 complex is targeted to its site of function by mRNA localization. Depletion of serum from culture medium inhibits Arp2/3-complex mRNA localization to the protrusion, whereas serum stimulation leads to significant mRNA localization within 30 minutes. The effect of serum suggests that Arp2/3-complex mRNA localization is a cellular response to extracellular stimuli. The localization of the Arp2/3 complex mRNAs is dependent on both actin filaments and microtubules, because disruption of either cytoskeletal system (with cytochalasin D and colchicine, respectively) inhibited the localization of all seven subunit mRNAs. In addition, myosin inhibitors significantly inhibit Arp2 mRNA localization in chicken embryo fibroblasts, suggesting a myosin motor dependent mechanism for Arp2/3-complex mRNA localization.
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