1,003 research outputs found

    The Allure of Celebrities: Unpacking Their Polysemic Consumer Appeal

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    The file attached to this record is the author's final peer reviewed version.To explain their deep resonance with consumers this paper unpacks the individual constituents of a celebrity’s polysemic appeal. While celebrities are traditionally theorised as unidimensional ‘semiotic receptacles of cultural meaning’, we conceptualise them here instead as human beings/performers with a multi-constitutional, polysemic consumer appeal. Supporting evidence is drawn from autoethnographic data collected over a total period of 25 months and structured through a hermeneutic analysis. In ‘rehumanising’ the celebrity, the study finds that each celebrity offers the individual consumer a unique and very personal parasocial appeal as a) the performer, b) the ‘private’ person behind the public performer, c) the tangible manifestation of either through products, and d) the social link to other consumers. The stronger these constituents, individually or symbiotically, appeal to the consumer’s personal desires the more s/he feels emotionally attached to this particular celebrity. Although using autoethnography means that the breadth of collected data is limited, the depth of insight this approach garners sufficiently unpacks the polysemic appeal of celebrities to consumers. The findings encourage talent agents, publicists and marketing managers to reconsider underlying assumptions in their talent management and/or celebrity endorsement practices. While prior research on celebrity appeal has tended to enshrine celebrities in a “dehumanised” structuralist semiosis, which erases the very idea of individualised consumer meanings, this paper reveals the multi-constitutional polysemy of any particular celebrity’s personal appeal as a performer and human being to any particular consumer

    "Am I as extended as you say I am?" Consumers' emic perspectives on the extended self

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    We would like to thank Pauline Maclaren (Editor) and each of the three reviewers of our work for their constructive comments and support throughout the review process. We would also like to thank Paula Gould and Grace Mackie for providing feedback on an earlier draft of this paper.Peer reviewedPostprin

    PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins

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    Integral peroxisomal membrane proteins (PMPs) are synthesized in the cytoplasm and imported posttranslationally. Here, we demonstrate that PEX19 binds and stabilizes newly synthesized PMPs in the cytosol, binds to multiple PMP targeting signals (mPTSs), interacts with the hydrophobic domains of PMP targeting signals, and is essential for PMP targeting and import. These results show that PEX19 functions as both a chaperone and an import receptor for newly synthesized PMPs. We also demonstrate the existence of two PMP import mechanisms and two classes of mPTSs: class 1 mPTSs, which are bound by PEX19 and imported in a PEX19-dependent manner, and class 2 mPTSs, which are not bound by PEX19 and mediate protein import independently of PEX19

    PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins

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    PEX19 is a chaperone and import receptor for newly synthesized, class I peroxisomal membrane proteins (PMPs). PEX19 binds these PMPs in the cytoplasm and delivers them to the peroxisome for subsequent insertion into the peroxisome membrane, indicating that there may be a PEX19 docking factor in the peroxisome membrane. Here we show that PEX3 is required for PEX19 to dock at peroxisomes, interacts specifically with the docking domain of PEX19, and is required for recruitment of the PEX19 docking domain to peroxisomes. PEX3 is also sufficient to dock PEX19 at heterologous organelles and binds PEX19 via a conserved motif that is essential for this docking activity and for PEX3 function in general. Not surprisingly, transient inhibition of PEX3 abrogates class I PMP import but has no effect on class II PMP import or peroxisomal matrix protein import. Taken together, these results suggest that PEX3 plays a selective, essential, and direct role in PMP import as a docking factor for PEX19

    New Approach to Silver Halide Photography Using Radical Cation Chemistry

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    A new mechanism for spectral sensitization of silver halide is described, which can potentially double the sensitivity of photographic emulsions. The photooxidized sensitizing dye is trapped using an organic donor molecule, which fragments to form a cation and a reducing radical, which injects an electron into the conduction band of the silver halide. In this way, two conduction-band electrons can be produced for each absorbed photon
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