Requirement of Microfilaments in Sorting of Actin Messenger RNA

Sundell, Cynthia L.; Singer, Robert H.

doi:10.1126/science.1891715

Cited by 240 publications

(156 citation statements)

References 27 publications

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“…Anchoring is defined here as the ability to bind mRNA to actin filaments in the correct location in vivo (Sundell and Singer, 1991). Either the targeting or the anchoring requires a 3Ј-UTR zipcode (Kislauskis et al, 1993.…”

Section: The Role Of Ef1␣ In Anchoring Versus Transport Of Mrnamentioning

confidence: 99%

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Interactions of Elongation Factor 1α with F-Actin and β-Actin mRNA: Implications for Anchoring mRNA in Cell Protrusions

Liu

Grant²,

Persky³

et al. 2002

MBoC

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160

159

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The targeting of mRNA and local protein synthesis is important for the generation and maintenance of cell polarity. As part of the translational machinery as well as an actin/ microtubule-binding protein, elongation factor 1␣ (EF1␣) is a candidate linker between the protein translation apparatus and the cytoskeleton. We demonstrate in this work that EF1␣ colocalizes with ␤-actin mRNA and F-actin in protrusions of chicken embryo fibroblasts and binds directly to F-actin and ␤-actin mRNA simultaneously in vitro in actin cosedimentation and enzyme-linked immunosorbent assays. To investigate the role of EF1␣ in mRNA targeting, we mapped the two actin-binding sites on EF1␣ at high resolution and defined one site at the N-terminal 49 residues of domain I and the other at the C-terminal 54 residues of domain III. In vitro actin-binding assays and localization in vivo of recombinant full-length EF1␣ and its various truncates demonstrated that the C terminus of domain III was the dominant actin-binding site both in vitro and in vivo. We propose that the EF1␣-F-actin complex is the scaffold that is important for ␤-actin mRNA anchoring. Disruption of this complex would lead to delocalization of the mRNA. This hypothesis was tested by using two dominant negative polypeptides: the actin-binding domain III of EF1␣ and the EF1␣-binding site of yeast Bni1p, a protein that inhibits EF1␣ binding to F-actin and also is required for yeast mRNA localization. We demonstrate that either domain III of EF1␣ or the EF1␣-binding site of Bni1p inhibits EF1␣ binding to ␤-actin mRNA in vitro and causes delocalization of ␤-actin mRNA in chicken embryo fibroblasts. Taken together, these results implicate EF1␣ in the anchoring of ␤-actin mRNA to the protrusion in crawling cells.

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Section: The Role Of Ef1␣ In Anchoring Versus Transport Of Mrnamentioning

confidence: 99%

“…The sorting of ␤-actin mRNA requires transport and then selective anchoring of the mRNA on the actin cytoskeleton in the lamella (Sundell and Singer, 1991). We have proposed that the mRNA is translated once it is anchored, to facilitate protein sorting (Kislauskis et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

Interactions of Elongation Factor 1α with F-Actin and β-Actin mRNA: Implications for Anchoring mRNA in Cell Protrusions

Liu

Grant²,

Persky³

et al. 2002

MBoC

Self Cite

160

159

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“…La synthèse locale d'actine, directement à proximité des sites de polymérisation, permet probablement de faciliter le processus [5][6][7]. Comme la localisation de l'ARNm de l'actine β est, dans les fibroblastes, dépendante des microfilaments d'actine eux-mêmes [9], l'ARNm de l'actine β est automatiquement transporté à proximité de la leading edge et une boucle de rétrocontrôle positive se met alors en place. Cette boucle pourrait ainsi faciliter un mouvement continu dans la même direction.…”

Section: Localisation Des Arnm De L'actine Et Polarisation De La Mobiunclassified

“…Les élements importants de ces déterminants peuvent être soit des structures secondaires et tertiaires plus ou moins complexes, soit des régions simple brin dont la séquence est alors critique. Les facteurs agissant en trans sur ces déterminants comprennent des protéines de reconnaissance de l'ARN, des protéines adaptatrices et, dans la très grande majorité des cas, un ou plusieurs éléments du cytosquelette [9]. Le rôle du cytosquelette est multiple : il peut à la fois servir de support pendant le transport de l'ARN et de point d'ancrage une fois l'ARN arrivé à destination.…”

Section: Mécanismes Généraux De Localisation Des Arnmunclassified

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Polarité cellulaire et localisation intracellulaire des ARNm de l’actine

Lavoie

Basyuk²,

Bordonne³

et al. 2004

Med Sci (Paris)

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Involvement of actin microfilaments in the transcription/replication of human parainfluenza virus type 3: Possible role of actin in other viruses

Banerjee

1999

Microsc. Res. Tech.

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Multifunctional involvement of actin microfilaments during viral infection has been documented in many studies. The molecular mechanism underlying this important host‐virus interaction, however, remains poorly understood. We have investigated the role of actin microfilaments in the life cycle of human parainfluenza virus type 3 (HPIV3), a paramyxovirus that causes severe respiratory illness in children. In vitro transcription with purified viral ribonucleoprotein (RNP) complex showed a requirement of cellular actin, in the polymeric form, for mRNA synthesis in vitro. This was further confirmed by using recombinant actin, which interacted with the viral RNP and also activated mRNA synthesis in vitro. Consistent with the role of the polymeric form of actin, the actin microfilaments of the cytoskeletal framework participate in the virus replication in vivo. Biochemical and immunological analyses revealed the association of viral RNPs with cytoskeletal framework during early stages of infection, and involvement of these RNPs in the synthesis of mRNAs and genome‐length RNA. Immunofluorescent labeling and confocal microscopy showed that the viral nucleocapsids colocalize with the actin microfilaments. Treatment of cells with cytochalasin D, which depolymerizes actin microfilaments, inhibited viral RNA synthesis and RNP accumulation. These data indicate that actin microfilaments play a critical role in HPIV3 life cycle, specifically at the level of viral transcription and replication. Involvement of the cytoskeletal framework in the life cycle of several viruses containing RNA and DNA genomes is reviewed. Microsc. Res. Tech. 47:114–123, 1999. © 1999 Wiley‐Liss, Inc.

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Requirement of Microfilaments in Sorting of Actin Messenger RNA

Cited by 240 publications

References 27 publications

Interactions of Elongation Factor 1α with F-Actin and β-Actin mRNA: Implications for Anchoring mRNA in Cell Protrusions

Interactions of Elongation Factor 1α with F-Actin and β-Actin mRNA: Implications for Anchoring mRNA in Cell Protrusions

Polarité cellulaire et localisation intracellulaire des ARNm de l’actine

Involvement of actin microfilaments in the transcription/replication of human parainfluenza virus type 3: Possible role of actin in other viruses

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