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(searched for: doi:10.1042/bss0740037)
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, Gleb P. Tolstykh, Melissa Tarango, Hope T. Beier, Bennett L. Ibey
Published: 11 January 2021
The Journal of Membrane Biology, Volume 254, pp 141-156; https://doi.org/10.1007/s00232-020-00160-z

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, Cory A. Olsovsky, Bennett L. Ibey,
Published: 1 April 2017
by SPIE
Journal: Neurophotonics
Neurophotonics, Volume 4, pp 025001-025001; https://doi.org/10.1117/1.nph.4.2.025001

Abstract:
Pulsed infrared (IR) laser energy has been shown to modulate neurological activity through both stimulation and inhibition of action potentials. While the mechanism(s) behind this phenomenon is (are) not completely understood, certain hypotheses suggest that the rise in temperature from IR exposure could activate temperature- or pressure-sensitive ion channels or create pores in the cellular outer membrane, allowing an influx of typically plasma-membrane-impermeant ions. Studies using fluorescent intensity-based calcium ion (Ca2+) sensitive dyes show changes in Ca2+ levels after various IR stimulation parameters, which suggests that Ca2+ may originate from the external solution. However, activation of intracellular signaling pathways has also been demonstrated, indicating a more complex mechanism of increasing intracellular Ca2+ concentration. We quantified the Ca2+ mobilization in terms of influx from the external solution and efflux from intracellular organelles using Fura-2 and a high-speed ratiometric imaging system that rapidly alternates the dye excitation wavelengths. Using nonexcitable Chinese hamster ovarian (CHO-hM1) cells and neuroblastoma-glioma (NG108) cells, we demonstrate that intracellular IP3 receptors play an important role in the IR-induced Ca2+, with the Ca2+ response augmented by ryanodine receptors in excitable cells.
Lorna S. Ehrlich, Gisselle N. Medina,
Published: 21 October 2011
Journal of Molecular Biology, Volume 413, pp 347-358; https://doi.org/10.1016/j.jmb.2011.08.038

Abstract:
Human immunodeficiency virus type 1 (HIV-1) release efficiency is directed by late (L) domain motifs in the viral structural precursor polyprotein Gag, which serve as links to the ESCRT (endosomal sorting complex required for transport) machinery. Linkage is normally through binding of Tsg101, an ESCRT-1 component, to the P7TAP motif in the p6 region of Gag. In its absence, budding is directed by binding of Alix, an ESCRT adaptor protein, to the LY36PXnL motif in Gag. We recently showed that budding requires activation of the inositol 1,4,5-triphosphate receptor (IP3R), a protein that “gates” Ca2+ release from intracellular stores, triggers Ca2+ cell influx and thereby functions as a major regulator of Ca2+ signaling. In the present study, we determined whether the L domain links Gag to Ca2+ signaling machinery. Depletion of IP3R and inactivation of phospholipase C (PLC) inhibited budding whether or not Tsg101 was bound to Gag. PLC hydrolysis of phosphatidylinositol-(4,5)-bisphosphate generates inositol (1,4,5)-triphosphate, the ligand that activates IP3R. However, with Tsg101 bound, Gag release was independent of Gq-mediated activation of PLC, and budding was readily enhanced by pharmacological stimulation of PLC. Moreover, IP3R was redistributed to the cell periphery and cytosolic Ca2+ was elevated, events indicative of induction of Ca2+ signaling. The results suggest that L domain function, ESCRT machinery and Ca2+ signaling are linked events in Gag release.
, Zhidan Luo, Shuangtao Ma, Daoyan Liu
Pflügers Archiv - European Journal of Physiology, Volume 461, pp 211-223; https://doi.org/10.1007/s00424-010-0902-5

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Niklas Engels, Lars Morten König, Christina Heemann, Johannes Lutz, Takeshi Tsubata, Sebastian Griep, Verena Schrader, Jürgen Wienands
Published: 9 August 2009
Nature Immunology, Volume 10, pp 1018-1025; https://doi.org/10.1038/ni.1764

Abstract:
The improved antibody responses of class-switched memory B cells depend on enhanced signaling from their B cell antigen receptors (BCRs). However, BCRs on both naive and antigen-experienced B cells use the canonical immunoglobulin-associated alpha and beta-protein signaling subunits. Here we identified a BCR isotype-specific signal-amplification mechanism. Whereas immunoglobulin M (IgM)-containing BCRs initiated intracellular signals exclusively through immunoglobulin-associated alpha- and beta-proteins, IgG- and IgE-containing BCRs also used a conserved tyrosine residue in the cytoplasmic segments of immunoglobulin heavy chains. When phosphorylated, this tyrosine recruited the adaptor Grb2, resulting in sustained protein kinase activation and prolonged generation of second messengers, which together culminated in enhanced B cell proliferation. Hence, membrane-bound IgG and IgE exert antigen recognition as well as costimulatory functions, thereby rendering memory B cells less dependent on T cell help.
Aida Ulloa, Albert L. Gonzales, Miao Zhong, Yoon-Sun Kim, Jeremy Cantlon, Colin Clay, Chun-Ying Ku, ,
Published: 31 July 2009
Journal: Cell calcium
Cell calcium, Volume 46, pp 73-84; https://doi.org/10.1016/j.ceca.2009.05.003

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, Mei-Hua Qu, Wei Ren, Hong-Zhen Hu, Na Gao, Guo-Du Wang, Xi-Yu Wang, Guijun Fei, Fei Zuo, Yun Xia, et al.
Published: 29 October 2008
Journal of Comparative Neurology, Volume 511, pp 847-862; https://doi.org/10.1002/cne.21874

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