25 research outputs found

    Men under pressure: representations of the `salaryman' and his organization in Japanese manga

    Get PDF
    In this article we analyse representations of the Japanese salaryman and Japanese organization in Japanese manga, or graphic novels, during the turbulent decades from the mid-1980s to the present day. We argue that manga presents salarymen protagonists in a sympathetic yet not uncritical light, and that it displays support for and criticism of both the Japanese and American organizational models. We describe how these manga offer important critical challenges from the world of popular culture to the direction of change in Japanese business organizations since the 1980s. In addition, we suggest that the manga may also provide salarymen with opportunities for critically re-evaluating their own working situations and for developing methods for surviving and thriving under the pressures of working within contemporary Japanese business organizations

    Distinct interactions stabilize EGFR dimers and higher-order oligomers in cell membranes

    No full text
    Summary: The epidermal growth factor receptor (EGFR) is a receptor tyrosine kinase with important roles in many cellular processes as well as in cancer and other diseases. EGF binding promotes EGFR dimerization and autophosphorylation through interactions that are well understood structurally. How these dimers relate to higher-order EGFR oligomers seen in cell membranes, however, remains unclear. Here, we used single-particle tracking (SPT) and Fƶrster resonance energy transfer imaging to examine how each domain of EGFR contributes to receptor oligomerization and the rate of receptor diffusion in the cell membrane. Although the extracellular region of EGFR is sufficient to drive receptor dimerization, we find that the EGF-induced EGFR slowdown seen by SPT requires higher-order oligomerizationā€”mediated in part by the intracellular tyrosine kinase domain when it adopts an active conformation. Our data thus provide important insight into the interactions required for higher-order EGFR assemblies involved in EGF signaling
    corecore