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Biochim Biophys Acta

Title:		Vestiges of Ent3p/Ent5p function in the giardial epsin homolog
Author(s):		Feliziani C; Valdez Taubas J; Moyano S; Quassollo G; Poprawski JE; Wendland B; Touz MC;
Address:		"Instituto de Investigacion Medica Mercedes y Martin Ferreyra, INIMEC-CONICET, Universidad Nacional de Cordoba, Friuli, 2434, Cordoba, Argentina. Centro de Investigaciones en Quimica Biologica de Cordoba, CIQUIBIC (UNC-CONICET), Departamento de Quimica Biologica, Facultad de Ciencias Quimicas, Universidad Nacional de Cordoba, Ciudad Universitaria, X5000HUA Cordoba, Argentina. Department of Biology, Johns Hopkins University, 3400 N. Charles St., Mudd Hall Room 35, Baltimore, USA. Instituto de Investigacion Medica Mercedes y Martin Ferreyra, INIMEC-CONICET, Universidad Nacional de Cordoba, Friuli, 2434, Cordoba, Argentina. Electronic address: ctouz@immf.uncor.edu"
Journal Title:		Biochim Biophys Acta
Year:		2016
Volume:		20160202
Issue:		4
Page Number:		749 - 759
DOI:		10.1016/j.bbamcr.2016.02.001
ISSN/ISBN:		0006-3002 (Print) 0006-3002 (Linking)
Abstract:		"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 ent1Deltaent2Delta mutant nor restored the GFP-Cps1 vacuolar trafficking defect in ent3Deltaent5Delta, 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 alpha-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"
Keywords:		"Adaptor Proteins, Vesicular Transport/chemistry/genetics/*physiology Amino Acid Sequence Animals *Evolution, Molecular Genes, Dominant Giardia lamblia/*genetics Humans Organisms, Genetically Modified Protein Structure, Tertiary/genetics Saccharomyces cere;"
Notes:		"MedlineFeliziani, Constanza Valdez Taubas, Javier Moyano, Sofia Quassollo, Gonzalo Poprawski, Joanna E Wendland, Beverly Touz, Maria C eng R01 GM060979/GM/NIGMS NIH HHS/ R01 GM60979/GM/NIGMS NIH HHS/ Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Netherlands 2016/02/07 Biochim Biophys Acta. 2016 Apr; 1863(4):749-59. doi: 10.1016/j.bbamcr.2016.02.001. Epub 2016 Feb 2"