Vestiges of Ent3p/Ent5p function in the giardial epsin homolog
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- 作者：Constanza Feliziania ; Javier Valdez Taubasb ; Sofí ; a Moyanoa ; Gonzalo Quassolloa ; Joanna E. Poprawskic ; Beverly Wendlandc ; 1 ; Maria C. Touza ; 1 ; ctouz@immf.uncor.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：GlENTHp ; Giardia lamblia ENTH protein ; CCVs ; clathrin-coated vesicles ; ENTH ; epsin N-terminal homology domain ; ANTH ; AP180 N-terminal homology domain ; VHS ; Vps27 ; Hrs and STAM domain ; UIMs ; ubiquitin-interaction motifs ; epsinR ; epsin related ; AP-1 ; adaptor protein complex ; CBM ; clathrin-binding motifs ; TGN ; trans-Golgi network ; 5-FAA ; 5-fluoroanthranilic acid ; Abp1 ; actin binding protein 1 ; Cps1 ; carboxypeptidase S
- 刊名：Biochimica et Biophysica Acta (BBA)-Molecular Cell Research
- 出版年：2016
- 出版时间：April 2016
- 年：2016
- 卷：1863
- 期：4
- 页码：749-759
- 全文大小：2653 K
文摘
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The protein GlENTHp (for Giardia lamblia ENTH protein) acts an Ent3/5p dominant-negative protein in Saccharomyces cerevisiae.
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GlENTHp impairs the correct clathrin-mediated trafficking between the TGN and the vacuole.
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GlENTHp might belong to the epsinR subfamily.
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20">A higher conservation of the protein sequence is required for proper function of the clathrin-coated machinery in yeast cells.