Global brand advertisements and the representation of localization in the example of Turkey

In the present-day world, globalization has increased the intensity of international competition, transforming the world into a single market. The concept of global advertisements, which gained importance parallel to globalization, is nowadays losing its status as the sole valid advertisement strategy for companies conducting business at a global level. The primary reason for this is the increasingly intense competition environment created by the entry of many new actors into the global and local markets, which has led global businesses to pay greater attention to the cultural variables of their target markets rather than just their economic variables.Culture represents all of the material and spiritual elements associated with a society, and can vary considerably from one society to another; in this context, culture is increasingly becoming the focus point of marketing and advertisements in the present-day world. One consequence of this new approach has been the entry of the concept of “glocal” into the advertisement literature.To summarize, the concept of “glocal” involves the creation advertisements that bear the characteristic and local cultural features of the country where they are broadcast, while also closely adhering to a general global concept and goal.This study focuses particularly on the representation of localization elements and prevailing ideologies in global brand advertisements in Turkey, a country that harbors a highly diverse multitude of different lifestyles, cultural backgrounds and traditions. This study evaluates local advertisement campaigns in Turkey for certain global brands according to their overall preferences and/or differences with respect to the local cultural elements they harbor and represent, and the ideological background for these preferences. This evaluationwas performed based on several advertisement examples/cases examined through semiological analysis methods.Keywords: Culture, Advertisements, cultural differences, Global Advertisement, Glocal Advertisement, Representation, Ideology.

In vitro reconstitution of an mRNA-transport complex reveals mechanisms of assembly and motor activation

The assembly and composition of ribonucleic acid (RNA)–transporting particles for asymmetric messenger RNA (mRNA) localization is not well understood. During mitosis of budding yeast, the Swi5p-dependent HO expression (SHE) complex transports a set of mRNAs into the daughter cell. We recombinantly reconstituted the core SHE complex and assessed its properties. The cytoplasmic precomplex contains only one motor and is unable to support continuous transport. However, a defined interaction with a second, RNA-bound precomplex after its nuclear export dimerizes the motor and activates processive RNA transport. The run length observed in vitro is compatible with long-distance transport in vivo. Surprisingly, SHE complexes that either contain or lack RNA cargo show similar motility properties, demonstrating that the RNA-binding protein and not its cargo activates motility. We further show that SHE complexes have a defined size but multimerize into variable particles upon binding of RNAs with multiple localization elements. Based on these findings, we provide an estimate of number, size, and composition of such multimeric SHE particles in the cell.

She3p Possesses a Novel Activity Required for ASH1 mRNA Localization in Saccharomyces cerevisiae

ABSTRACT Intracellular and intercellular polarity requires that specific proteins be sorted to discreet locations within and between cells. One mechanism for sorting proteins is through RNA localization. In Saccharomyces cerevisiae, ASH1 mRNA localizes to the distal tip of the bud, resulting in the asymmetric sorting of the transcriptional repressor Ash1p. ASH1 mRNA localization requires four cis-acting localization elements and the trans-acting factors Myo4p, She3p, and She2p. Myo4p is a type V myosin motor that functions to directly transport ASH1 mRNA to the bud. She2p is an RNA-binding protein that directly interacts with the ASH1 mRNA cis-acting elements. Currently, the role for She3p in ASH1 mRNA localization is as an adaptor protein, since it can simultaneously associate with Myo4p and She2p. Here, we present data for two novel mutants of She3p, S348E and the double mutant S343E S361E, that are defective for ASH1 mRNA localization, and yet both of these mutants retain the ability to associate with Myo4p and She2p. These observations suggest that She3p possesses a novel activity required for ASH1 mRNA localization, and our data imply that this function is related to the ability of She3p to associate with ASH1 mRNA. Interestingly, we determined that She3p is phosphorylated, and global mass spectrometry approaches have determined that Ser 343, 348, and 361 are sites of phosphorylation, suggesting that the novel function for She3p could be negatively regulated by phosphorylation. The present study reveals that the current accepted model for ASH1 mRNA localization does not fully account for the function of She3p in ASH1 mRNA localization.