کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10801780 | 1055635 | 2016 | 36 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Vestiges of Ent3p/Ent5p function in the giardial epsin homolog
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کلمات کلیدی
UIMsAP-1CPS1CCVsVHSTGNadaptor protein complexCBMABP1Endocytosis - آندوسیتوز یا درون بریEnth - انهVesicle transport - حمل و نقل VesicleVacuole - خلاص شدن از شرAnth - دومTrans-Golgi network - شبکه Trans-GoljiGiardia lamblia - لامبلیا ژیاردیاYeast - مخمرclathrin-coated vesicles - کیسه های کلاچری پوشش داده شده
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
An accurate way to characterize the functional potential of a protein is to analyze recognized protein domains encoded by the genes in a given group. The epsin N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated trafficking. In this work, we investigate the function of the single ENTH-containing protein from the protist Giardia lamblia by testing its function in Saccharomyces cerevisiae. This protein, named GlENTHp (for G. lamblia ENTH protein), is involved in Giardia in endocytosis and in protein trafficking from the ER to the vacuoles, fulfilling the function of the ENTH proteins epsin and epsinR, respectively. There are two orthologs of epsin, Ent1p and Ent2p, and two orthologs of epsinR, Ent3p and Ent5p in S. cerevisiae. Although the expression of GlENTHp neither complemented growth in the ent1Îent2Î mutant nor restored the GFP-Cps1 vacuolar trafficking defect in ent3Îent5Î, it interfered with the normal function of Ent3/5 in the wild-type strain. The phenotype observed is linked to a defect in Cps1 localization and α-factor mating pheromone maturation. The finding that GlENTHp acts as dominant negative epsinR in yeast cells reinforces the phylogenetic data showing that GlENTHp belongs to the epsinR subfamily present in eukaryotes prior to their evolution into different taxa.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1863, Issue 4, April 2016, Pages 749-759
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1863, Issue 4, April 2016, Pages 749-759
نویسندگان
Constanza Feliziani, Javier Valdez Taubas, SofÃa Moyano, Gonzalo Quassollo, Joanna E. Poprawski, Beverly Wendland, Maria C. Touz,