Role of H(abc) domain in membrane trafficking and targeting of syntaxin 1A |
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Authors: | Fan Junmei Yang Xiaofei Lu Jingze Chen Liangyi Xu Pingyong |
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Institution: | Joint Laboratory of the Institute of Biophysics & Huazhong University of Science and Technology, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China. |
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Abstract: | Membrane syntaxin plays essential roles in exocytosis in eukaryotic cells. The conservative H(abc) domain in plasma membrane syntaxins implies important roles for syntaxin targeting and function. Our previous study showed H(abc) domain was necessary for the trafficking and cluster distribution of syntaxin 1A on the plasma membrane. Here we identified which of the three domains (H(a), H(b) and H(c)) was essential for Stx1A trafficking and clustering. We found that, in INS-1 cells, the mutant truncated with either H(a), H(b) or H(c) domain could be sorted to the cell surface by a different mechanism compared to that of whole H(abc) truncated mutant. In contrast to wild type Stx1A, none of the mutants showed cluster distribution at the functional sites, suggesting that the physiological localization of Stx1A relies on intact H(abc) domain. Furthermore Munc18-1 is found not to be essential for Stx1A cluster distribution, despite important role in stabilizing membrane delivery of Stx1A. |
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Keywords: | SNARE soluble N-ethylmaleimide-sensitive factor attachment protein receptor CHO Chinese hamster ovary t-SNARE target membrane SNARE v-SNARE vesicle-associated SNARE Stx1A syntaxin 1A ER endoplasmic reticulum TMD transmembrane domain TIRFM total internal reflection fluorescence microscopy GFP green fluorescence protein EGFP enhanced GFP RFP red fluorescence protein IRES internal ribosome entry site BoNT/E botulinum neurotoxin type E |
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