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The septin cytoskeleton facilitates membrane retraction during motility and blebbing.
Increasing evidence supports a critical role for the septin cytoskeleton at the plasma membrane during physiological processes including motility, formation of dendritic spines or cilia, and phagocytosis. We sought to determine how septins regulate the plasma membrane, focusing on this cytoskeletal element's role during effective amoeboid motility. Surprisingly, septins play a reactive rather than proactive role, as demonstrated during the response to increasing hydrostatic pressure and subsequent regulatory volume decrease. In these settings, septins were required for rapid cortical contraction, and SEPT6-GFP was recruited into filaments and circular patches during global cortical contraction and also specifically during actin filament depletion. Recruitment of septins was also evident during excessive blebbing initiated by blocking membrane trafficking with a dynamin inhibitor, providing further evidence that septins are recruited to facilitate retraction of membranes during dynamic shape change. This function of septins in assembling on an unstable cortex and retracting aberrantly protruding membranes explains the excessive blebbing and protrusion observed in septin-deficient T cells
Bose-Einstein condensation in strong-coupling quark color superconductor near flavor SU(3) limit
Near the flavor SU(3) limit, we propose an analytical description for
color-flavor-locked-type Bardeen-Cooper-Schrieffer (BCS) phase in the Nambu
Jona-Lasinio (NJL) model. The diquark behaviors in light-flavor and
strange-flavor-involved channels and Bose-Einstein condensation (BEC) of bound
diquark states are studied. When the attractive interaction between quarks is
strong enough, a BCS-BEC crossover is predicted in the environment with
color-flavor-locked pairing pattern. The resulting Bose-Einstein condensed
phase is found to be an intergrade phase before the emergence of the
previous-predicted BEC phase in two-flavor quark superconductor.Comment: 15 pages, 5 figures; 2nd versio
How Does Social Media Interactivity Affect Brand Loyalty?
As social media has become a prominent platform for networking, many organizations have begun to establish more than one brand community, as a set of supplements to their branded websites. Once most online brand interactions take place on social networking sites rather than branded sites, such customer-oriented interactions will become much more complicated and unpredictable. It is a real challenge for organizations to build successful customer-brand relationships through social networking sites. Hence, organizations that wish to enhance brand loyalty by running brand communities face the challenge of effectively conducting social customer relationship management (CRM) tactics. As social media users are susceptible to highly interactive features, understanding the nature of social media interactivity in brand communities is the key to building successful social CRM. The aim of the study is to investigate not only the effect of social media interactivity on community benefits, but also the effect of community benefits on brand loyalty. In addition to measuring the direct effects of social influence and media richness on brand loyalty, the study assessed the indirect effect of responsiveness on brand loyalty by means of community benefits, including knowledge gains and sense of membership. The results, based on data collected from 229 social media users who are followers of a Super Basketball League (SBL) team’s Facebook page, indicated that media richness had a strong, positive, and direct effect on brand loyalty, and that responsiveness had direct effects on their knowledge gains and their sense of membership, which in turn affected brand loyalty indirectly
Thin-film 'Thermal Well' Emitters and Absorbers for High-Efficiency Thermophotovoltaics
A new approach is introduced to significantly improve the performance of
thermophotovoltaic (TPV) systems by using low-dimensional thermal emitters and
photovoltaic (PV) cells. By reducing the thickness of both the emitter and the
PV cell, strong spectral selectivity in both thermal emission and absorption
can be achieved by confining photons in trapped waveguide modes inside the
thin-films that act as thermal analogs to quantum wells. Simultaneously,
photo-excited carriers travel shorter distances across the thin-films reducing
bulk recombination losses resulting in a lower saturation current in the PV
cell. We predict a TPV efficiency enhancement with near-field coupling between
the thermal emitter and the PV cell of up to 38.7% using a germanium (Ge)
emitter at 1000 K and a gallium antimonide (GaSb) cell with optimized
thicknesses separated by 100 nm. Even in the far-field limit, the efficiency is
predicted to reach 31.5%, which is an order of magnitude higher than the
Shockley Queisser limit of 1.6% for a bulk GaSb cell and a blackbody emitter at
1000 K. The proposed design approach does not require nanoscale patterning of
the emitter and PV cell surfaces, but instead offers a simple low-cost solution
to improve the performance of a thermophotovoltaic system.Comment: Manuscript and supplementary informatio
The integrin-binding defective FGF2 mutants potently suppress FGF2 signalling and angiogenesis.
We recently found that integrin αvβ3 binds to fibroblast growth factor (FGF)-αvβ31 (FGF1), and that the integrin-binding defective FGF1 mutant (Arg-50 to glutamic acid, R50E) is defective in signalling and antagonistic to FGF1 signalling. R50E suppressed angiogenesis and tumour growth, suggesting that R50E has potential as a therapeutic. However, FGF1 is unstable, and we had to express R50E in cancer cells for xenograft study, since injected R50E may rapidly disappear from circulation. We studied if we can develop antagonist of more stable FGF2. FGF2 is widely involved in important biological processes such as stem cell proliferation and angiogenesis. Previous studies found that FGF2 bound to αvβ3 and antagonists to αvβ3 suppressed FGF2-induced angiogenesis. However, it is unclear how FGF2 interacts with integrins. Here, we describe that substituting Lys-119/Arg-120 and Lys-125 residues in the predicted integrin-binding interface of FGF2 to glutamic acid (the K119E/R120E and K125E mutations) effectively reduced integrin binding to FGF2. These FGF2 mutants were defective in signalling functions (ERK1/2 activation and DNA synthesis) in NIH3T3 cells. Notably they suppressed, FGF2 signalling induced by WT FGF2 in endothelial cells, suggesting that the FGF2 mutants are antagonists. The FGF2 mutants effectively suppressed tube formation in vitro, sprouting in aorta ring assays ex vivo and angiogenesis in vivo The positions of amino acids critical for integrin binding are different between FGF1 and FGF2, suggesting that they do not interact with integrins in the same manner. The newly developed FGF2 mutants have potential as anti-angiogenic agents and useful tools for studying the role of integrins in FGF2 signalling
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