Gene Symbol: Ent3p
Description: Ent3p
Alias: Ent3p
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Pruyne D, Bretscher A. Polarization of cell growth in yeast. J Cell Sci. 2000;113 ( Pt 4):571-85 pubmed
    ..The dynamic arrangement of targeting and recycling provides flexibility for the precise control of morphogenesis. ..
  2. Friant S, Pécheur E, Eugster A, Michel F, Lefkir Y, Nourrisson D, et al. Ent3p Is a PtdIns(3,5)P2 effector required for protein sorting to the multivesicular body. Dev Cell. 2003;5:499-511 pubmed
    ..Here we show that Ent3p, a yeast epsin N-terminal homology (ENTH) domain-containing protein, is a specific PtdIns(3,5)P(2) effector ..
  3. Chidambaram S, Müllers N, Wiederhold K, Haucke V, von Mollard G. Specific interaction between SNAREs and epsin N-terminal homology (ENTH) domains of epsin-related proteins in trans-Golgi network to endosome transport. J Biol Chem. 2004;279:4175-9 pubmed
    ..Yeast Vti1p interacted with the ENTH domain of Ent3p. ENTH proteins are involved in the formation of clathrin-coated vesicles...
  4. Eugster A, Pécheur E, Michel F, Winsor B, Letourneur F, Friant S. Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. Mol Biol Cell. 2004;15:3031-41 pubmed
    ..We show that Ent5p, a yeast protein of the epsin family homologous to Ent3p, localizes to endosomes and specifically binds to PtdIns(3,5)P(2) via its ENTH domain...
  5. Costaguta G, Duncan M, Fernandez G, Huang G, Payne G. Distinct roles for TGN/endosome epsin-like adaptors Ent3p and Ent5p. Mol Biol Cell. 2006;17:3907-20 pubmed
    ..We observed that epsin-like protein Ent3p preferentially localized with Gga2p, whereas Ent5p distributed equally between AP-1 and Gga2p...
  6. Zimmermann J, Chidambaram S, Fischer von Mollard G. Dissecting Ent3p: the ENTH domain binds different SNAREs via distinct amino acid residues while the C-terminus is sufficient for retrograde transport from endosomes. Biochem J. 2010;431:123-34 pubmed publisher
    The ENTH (epsin N-terminal homology) domain protein Ent3p and the ANTH [AP (adaptor protein)-180 N-terminal homology] domain protein Ent5p serve as partially redundant adaptors in vesicle budding from the TGN (trans-Golgi network) in ..
  7. Wendland B, Steece K, Emr S. Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis. EMBO J. 1999;18:4383-93 pubmed
    ..Based on these and other data, we propose that the yeast epsin-like proteins are essential components of an endocytic complex that may act at multiple stages in the endocytic pathway. ..
  8. Duncan M, Costaguta G, Payne G. Yeast epsin-related proteins required for Golgi-endosome traffic define a gamma-adaptin ear-binding motif. Nat Cell Biol. 2003;5:77-81 pubmed
    ..Here we describe two epsin amino-terminal homology (ENTH) domain-containing proteins, Ent3p and Ent5p, that are intimately involved in clathrin function at the Golgi...
  9. Copic A, Starr T, Schekman R. Ent3p and Ent5p exhibit cargo-specific functions in trafficking proteins between the trans-Golgi network and the endosomes in yeast. Mol Biol Cell. 2007;18:1803-15 pubmed
    The phosphoinositide-binding proteins Ent3p and Ent5p are required for protein transport from the trans-Golgi network (TGN) to the vacuole in Saccharomyces cerevisiae...

More Information


  1. Fang P, Li X, Wang J, Niu L, Teng M. Structural basis for the specificity of the GAE domain of yGGA2 for its accessory proteins Ent3 and Ent5 . Biochemistry. 2010;49:7949-55 pubmed publisher
    ..These results suggest accessory proteins may fine-tune the GGA adaptor dependence by adjusting their non-acidic-phenylalanine residues, thus contributing to the distinct role of Ent3 and Ent5 in trafficking. ..
  2. Wang J, Gossing M, Fang P, Zimmermann J, Li X, von Mollard G, et al. Epsin N-terminal homology domains bind on opposite sides of two SNAREs. Proc Natl Acad Sci U S A. 2011;108:12277-82 pubmed publisher
    ..Here, we report the recognition between yeast SNARE Vti1p and its adaptor Ent3p derived from three crystal structures...