کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10753606 | 1050344 | 2015 | 39 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Arabidopsis dynamin-related proteins, DRP2A and DRP2B, function coordinately in post-Golgi trafficking
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کلمات کلیدی
CLSMY2HBiFCDrp2Latrunculin BGEDPRDDRPPtdInsTGNSH3Arabidopsis - آرابیدوپسیس یا رشادیOryzalin - اوریزینProline-rich domain - دامنه غنی پرولینTrans-Golgi network - شبکه Trans-GoljiPearson’s correlation coefficient - ضریب همبستگی پیرسونPlasma membrane - غشای پلاسماphosphatidylinositol - فسفاتیدیل اینوزیتولPhosphoinositide - فسفوئوزیتیدyeast two-hybrid - مخمر دو رقمیconfocal laser scanning microscopy - میکروسکوپهای اسکن لیزری کانفوکالSrc homology 3 - همبستگی Src 3Pleckstrin Homology - همخوانی Pleckstrinwortmannin - ورتمنینDynamin-related protein - پروتئین مربوط به دینامین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Dynamin-related proteins (DRPs) are large GTPases involved in a wide range of cellular membrane remodeling processes. In Arabidopsis thaliana, two paralogous land plant-specific type DRPs, DRP2A and DRP2B, are thought to participate in the regulation of post-Golgi trafficking. Here, we examined their molecular properties and functional relationships. qRT-PCR and GUS assays showed that DRP2A and DRP2B were expressed ubiquitously, although their expressions were strongest around root apical meristems and vascular bundles. Yeast two-hybrid, bi-molecular fluorescent complementation, and co-immunoprecipitation mass spectrometry analyses revealed that DRP2A and DRP2B interacted with each other. In observations with confocal laser scanning microscopy and variable incidence angle fluorescent microscopy, fluorescent fusions of DRP2A and DRP2B almost completely co-localized and were mainly localized to endocytic vesicle formation sites of the plasma membrane, clathrin-enriched trans-Golgi network and the cell plate in root epidermal cells. Treatments with wortmannin, an inhibitor of phosphatidylinositol 3-/4-kinases, latrunculin B, an inhibitor of actin polymerization, and oryzalin, an inhibitor of microtubule polymerization, increased the resident time of DRP2A and DRP2B on the plasma membrane. These results show that DRP2A and DRP2B function coordinately in multiple pathways of post-Golgi trafficking in phosphatidylinositol 3- or 4-kinase and cytoskeleton polymerization-dependent manners.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 456, Issue 1, 2 January 2015, Pages 238-244
Journal: Biochemical and Biophysical Research Communications - Volume 456, Issue 1, 2 January 2015, Pages 238-244
نویسندگان
Jiahe Huang, Masaru Fujimoto, Masayuki Fujiwara, Yoichiro Fukao, Shin-ichi Arimura, Nobuhiro Tsutsumi,