Actin mRNA localizes in the absence of protein synthesis.

Sundell, Cynthia L.; Singer, Robert H.

doi:10.1083/jcb.111.6.2397

Cited by 103 publications

(73 citation statements)

References 33 publications

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“…The sorting of mRNA for the actin isoforms provides an interesting system to study the mRNA localization machinery (Singer, 1992). Actin mRNA distribution depends on a pre-existing actinbased filament because the disruption of this network by cytochalasin, but not colcemid, alters its subcellular localization (Sundell and Singer, 1990). More recently, Singer's group revealed two nucleotide segments, within ,B-actin mRNA, that are responsible for the ,3-actin mRNA localization and for the cell phenotype determination .…”

Section: Discussionmentioning

confidence: 99%

Polarized distribution of actin isoforms in gastric parietal cells.

Yao

Chaponnier

Gabbiani

et al. 1995

MBoC

109

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The actin genes encode several structurally similar, but perhaps functionally different, protein isoforms that mediate contractile function in muscle cells and determine the morphology and motility in nonmuscle cells. To reveal the isoform profile in the gastric monomeric actin pool, we purified actin from the cytosol of gastric epithelial cells by DNase I affinity chromatography followed by two-dimensional gel electrophoresis. Actin isoforms were identified by Western blotting with a monoclonal antibody against all actin isoforms and two isoform-specific antibodies against cytoplasmic ,B-actin and -y-actin. Densitometry revealed a ratio for f3-actin/ y-actin that equaled 0.73 + 0.09 in the cytosol. To assess the distribution of actin isoforms in gastric glandular cells in relation to ezrin, a putative membrane-cytoskeleton linker, we carried out double immunofluorescence using actin-isoform-specific antibodies and ezrin antibody. Immunostaining confirmed that ezrin resides mainly in canaliculi and apical plasma membrane of parietal cells. Staining for the ,B-actin isoform was intense along the entire gland lumen and within the canaliculi of parietal cells, thus predominantly near the apical membrane of all gastric epithelial cells, although lower levels of ,B-actin were also identified near the basolateral membrane. The y-actin isoform was distributed heavily near the basolateral membrane of parietal cells, with much less intense staining of parietal cell canaliculi and no staining of apical membranes. Within parietal cells, the cellular localization of ,B-actin, but not y-actin, isoform superimposed onto that of ezrin. In a search for a possible selective interaction between actin isoforms and ezrin, we carried out immunoprecipitation experiments on gastric membrane extracts in which substantial amounts of actin were co-eluted with ezrin from an anti-ezrin affinity column. The ratio of 13-actin/ y-actin in the immunoprecipitate (3/,y = 2.14 + 0.32) was significantly greater than that found in the cytosolic fraction. In summary, we have shown that ,B-and 'y-actin isoforms are differentially distributed in gastric parietal cells. Furthermore, our data suggest a preferential, but not exclusive, interaction between 1B-actin and ezrin in gastric parietal cells.Finally, our results suggest that the ,B-and y-actin-based cytoskeleton networks might function separately in response to the stimulation of acid secretion. INTRODUCTION essential role in a variety of cellular processes such as maintaining cell shape, cell motility, and cytokinesis.

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Section: Discussionmentioning

confidence: 99%

Polarized distribution of actin isoforms in gastric parietal cells.

Yao

Chaponnier

Gabbiani

et al. 1995

MBoC

109

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“…In addition, forskolin did not change the partitioning of/5-actin mRNA between detergent soluble and cytoskeletal fractions, with the majority of the mRNA remaining associated with the cytoskeleton. Depolymerization of actin filaments by cytochalasin D resuits in both delocalization of/~-actin mRNA (Sundell and Singer, 1990) and the release of most poly (A) mRNA from the cytoskeleton (Ornelles et al, 1986;Taneja et al, 1992). Therefore forskolin delocalized mRNA is not freely diffusible or released from the cytoskeleton.…”

Section: Discussionmentioning

confidence: 99%

“…Eight oligonucleotide probes specific to chick ~-actin mRNA were synthesized and end labeled with digoxigenin-dUTP. Digoxigeninlabeled nick-translated probes were prepared as described (Sundell and Singer, 1990). The eDNA probe used was a 1.38-kb segment (nucleotide 95-1477) of a full-length ~-actin cDNA probe (Cleveland et al, 1980).…”

Section: Detection Of ~-Actin Mrna By In Situ Hybridizationmentioning

confidence: 99%

“…Peripheral localization of B-actin mRNA does not require ongoing protein synthesis (Sundell and Singer, 1990) and is mediated by an interaction between B-actin mRNA and the actin-based cytoskeletal framework (Sundell and Singer, 1991). Since signal transduction mechanisms mediate the functionally related events of growth factor stimulation; ~gytoskeletal reorganization and directional cellular motility .…”

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confidence: 99%

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Beta-actin mRNA localization is regulated by signal transduction mechanisms.

Latham

Kislauskis

Singer

et al. 1994

The Journal of Cell Biology

Self Cite

125

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A b s t r a c t . B-actin mRNA is localized in the leading lamellae of chicken embryo fibroblasts (CEFs) (Lawrence, J., and R. Singer. 1986. Cell. 45:407-415), close to where actin polymerization in the lamellipodia drives cellular motility. During serum starvation B-actin mRNA becomes diffuse and nonlocalized. Addition of FCS induces a rapid (within 2-5 min) redistribution of B-actin mRNA into the leading lamellae. A similar redistribution was seen with PDGF, a fibroblast chemotactic factor. PDGFinduced B-actin mRNA redistribution was inhibited by the tyrosine kinase inhibitor herbimycin, indicating that this process requires intact tyrosine kinase activity, similar to actin filament polymerization and chemotaxis. Lysophosphatidic acid, which has been shown to rapidly induce actin stress fiber formation (Ridley, A., and A. Hall. 1992. Cell. 790:389-399), also increases peripheral B-actin mRNA localization within minutes. This suggests that actin polymerization and mRNA localization may be regulated by similar signaling pathways. Additionally, activators or inhibitors of kinase A or C can also delocalize steady-state B-actin mRNA in cells grown in serum, and can inhibit the serum induction of peripherally localized B-actin mRNA in serum-starved CEFs. These data show that physiologically relevant extracellular factors operating through a signal transduction pathway can regulate spatial sites of actin protein synthesis, which may in turn affect cellular polarity and motility.

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“…In polarized somatic cells and during early vertebrate development, endogenous RNAs are observed as large granules (Barbarese et al, 1995;Ainger et al, 1997;Carson et al, 1998;Rook et al, 2000;Krichevsky and Kosik, 2001) or particles (Sundell and Singer, 1990;Ferrandon et al, 1994;Forristall et al, 1995;Kloc and Etkin, 1995) that move at rates ranging from 4 to 6 m/min via cytoskeleton-associated motors (Bassell and Singer, 1997;Chartrand et al, 2001;Saxton, 2001;Kloc et al, 2002;Tekotte and Davis, 2002). When microinjected in oligodendrocytes, fluorescently labeled myelin basic protein RNA first condenses into granules that then move along microtubule tracks to the peripheral extensions, where they are localized (Ainger et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

The Transport of Prolamine RNAs to Prolamine Protein Bodies in Living Rice Endosperm Cells[W]

et al. 2003

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RNAs that code for the major rice storage proteins are localized to specific subdomains of the cortical endoplasmic reticulum (ER) in developing endosperm. Prolamine RNAs are localized to the ER and delimit the prolamine intracisternal inclusion granules (PB-ER), whereas glutelin RNAs are targeted to the cisternal ER. To study the transport of prolamine RNAs to the surface of the prolamine protein bodies in living endosperm cells, we adapted a two-gene system consisting of green fluorescent protein (GFP) fused to the viral RNA binding protein MS2 and a hybrid prolamine RNA containing tandem MS2 RNA binding sites. Using laser scanning confocal microscopy, we show that the GFP-labeled prolamine RNAs are transported as particles that move at an average speed of 0.3 to 0.4 m/s. These prolamine RNA transport particles generally move unidirectionally in a stop-and-go manner, although nonlinear bidirectional, restricted, and nearly random movement patterns also were observed. Transport is dependent on intact microfilaments, because particle movement is inhibited rapidly by the actin filament-disrupting drugs cytochalasin D and latrunculin B. Direct evidence was obtained that these prolamine RNA-containing particles are transported to the prolamine protein bodies. The significance of these results with regard to protein synthesis in plants is discussed.

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Actin mRNA localizes in the absence of protein synthesis.

Cited by 103 publications

References 33 publications

Polarized distribution of actin isoforms in gastric parietal cells.

Polarized distribution of actin isoforms in gastric parietal cells.

Beta-actin mRNA localization is regulated by signal transduction mechanisms.

The Transport of Prolamine RNAs to Prolamine Protein Bodies in Living Rice Endosperm Cells[W]

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