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Lívia A S Carmo, Felipe F Dias, Kássia K Malta, Kátia B Amaral, Revital Shamri, Peter F Weller, Rossana C N Melo
BACKGROUND: SNARE members mediate membrane fusion during intracellular trafficking underlying innate and adaptive immune responses by different cells. However, little is known about the expression and function of these proteins in human eosinophils, cells involved in allergic, inflammatory and immunoregulatory responses. Here, we investigate the expression and distribution of the Qa-SNARE syntaxin17 (STX17) within human eosinophils isolated from the peripheral blood. METHODS: Flow cytometry and a pre-embedding immunonanogold electron microscopy (EM) technique that combines optimal epitope preservation and secondary Fab-fragments of antibodies linked to 1...
October 1, 2015: Experimental Cell Research
Xiu-Tang Cheng, Bing Zhou, Mei-Yao Lin, Qian Cai, Zu-Hang Sheng
Efficient degradation of autophagic vacuoles (AVs) via lysosomes is an important cellular homeostatic process. This is particularly challenging for neurons because mature acidic lysosomes are relatively enriched in the soma. Although dynein-driven retrograde transport of AVs was suggested, a fundamental question remains how autophagosomes generated at distal axons acquire dynein motors for retrograde transport toward the soma. In this paper, we demonstrate that late endosome (LE)-loaded dynein-snapin complexes drive AV retrograde transport in axons upon fusion of autophagosomes with LEs into amphisomes...
May 11, 2015: Journal of Cell Biology
Binbin Ding, Guangyuan Zhang, Xiaodan Yang, Shengwei Zhang, Longyun Chen, Qin Yan, Mengyao Xu, Amiya K Banerjee, Mingzhou Chen
Autophagy is a multistep process in which cytoplasmic components, including invading pathogens, are captured by autophagosomes that subsequently fuse with degradative lysosomes. Negative-strand RNA viruses, including paramyxoviruses, have been shown to alter autophagy, but the molecular mechanisms remain largely unknown. We demonstrate that human parainfluenza virus type 3 (HPIV3) induces incomplete autophagy by blocking autophagosome-lysosome fusion, resulting in increased virus production. The viral phosphoprotein (P) is necessary and sufficient to inhibition autophagosome degradation...
May 14, 2014: Cell Host & Microbe
Szabolcs Takáts, Péter Nagy, Ágnes Varga, Karolina Pircs, Manuéla Kárpáti, Kata Varga, Attila L Kovács, Krisztina Hegedűs, Gábor Juhász
During autophagy, phagophores capture portions of cytoplasm and form double-membrane autophagosomes to deliver cargo for lysosomal degradation. How autophagosomes gain competence to fuse with late endosomes and lysosomes is not known. In this paper, we show that Syntaxin17 is recruited to the outer membrane of autophagosomes to mediate fusion through its interactions with ubisnap (SNAP-29) and VAMP7 in Drosophila melanogaster. Loss of these genes results in accumulation of autophagosomes and a block of autolysosomal degradation during basal, starvation-induced, and developmental autophagy...
May 13, 2013: Journal of Cell Biology
Madhavi Muppirala, Vijay Gupta, Ghanshyam Swarup
The T-cell protein tyrosine phosphatase is expressed as two splice variants - TC45, a nuclear protein, and TC48, which is localized predominantly in the ER (endoplasmic reticulum). Yeast two-hybrid screening revealed direct interaction of TC48 with Syntaxin17, a SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein localized predominantly in the ER and to some extent in the ER-Golgi intermediate compartment. Syntaxin 17 did not interact with TC45. C-terminal 40 amino acids of TC48 were sufficient for interaction with syntaxin 17...
December 2012: Biochimica et Biophysica Acta
Silke Stertz, Mike Reichelt, Jacomine Krijnse-Locker, Jason Mackenzie, Jeremy C Simpson, Otto Haller, Georg Kochs
Human MxA protein belongs to the superfamily of dynamin-like large GTPases that are involved in intracellular membrane trafficking. MxA is induced by interferons-alpha/beta (IFN-alpha/beta) and is a key component of the antiviral response against RNA viruses. Here, we show that MxA localizes to membranes that are positive for specific markers of the smooth endoplasmic reticulum, such as Syntaxin17, but is excluded from other membrane compartments. Overexpression of MxA leads to a characteristic reorganization of the associated membranes...
September 2006: Journal of Interferon & Cytokine Research
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