EH Domain-Containing Protein 1

2020 ◽  
Author(s):  
Keyword(s):  
Eh Domain

scholarly journals Regulation of clathrin coat assembly by Eps15 homology domain–mediated interactions during endocytosis

2012 ◽  
Vol 23 (4) ◽  
pp. 687-700 ◽  
Author(s):  
Ryohei Suzuki ◽  
Junko Y. Toshima ◽  
Jiro Toshima
Keyword(s):  
Functional Diversity ◽  
Protein Interaction ◽  
Interaction Domain ◽  
Protein Protein Interaction ◽  
Molecular Events ◽  
Biological Studies ◽  
Eh Domain ◽  
Actin Patch ◽  
Lines Of Evidence

Clathrin-mediated endocytosis involves a coordinated series of molecular events regulated by interactions among a variety of proteins and lipids through specific domains. One such domain is the Eps15 homology (EH) domain, a highly conserved protein–protein interaction domain present in a number of proteins distributed from yeast to mammals. Several lines of evidence suggest that the yeast EH domain–containing proteins Pan1p, End3p, and Ede1p play important roles during endocytosis. Although genetic and cell-biological studies of these proteins suggested a role for the EH domains in clathrin-mediated endocytosis, it was unclear how they regulate clathrin coat assembly. To explore the role of the EH domain in yeast endocytosis, we mutated those of Pan1p, End3p, or Ede1p, respectively, and examined the effects of single, double, or triple mutation on clathrin coat assembly. We found that mutations of the EH domain caused a defect of cargo internalization and a delay of clathrin coat assembly but had no effect on assembly of the actin patch. We also demonstrated functional redundancy among the EH domains of Pan1p, End3p, and Ede1p for endocytosis. Of interest, the dynamics of several endocytic proteins were differentially affected by various EH domain mutations, suggesting functional diversity of each EH domain.

scholarly journals Pan1p, End3p, and Sla1p, Three Yeast Proteins Required for Normal Cortical Actin Cytoskeleton Organization, Associate with Each Other and Play Essential Roles in Cell Wall Morphogenesis

2000 ◽  
Vol 20 (1) ◽  
pp. 12-25 ◽  
Author(s):  
Hsin-Yao Tang ◽  
Jing Xu ◽  
Mingjie Cai
Keyword(s):  
Cell Wall ◽  
Actin Cytoskeleton ◽  
Normal Cell ◽  
Cell Cortex ◽  
Repeat Region ◽  
Cortical Actin ◽  
Cytoskeleton Organization ◽  
Eh Domain ◽  
Actin Cytoskeleton Organization ◽  
Cell Wall Morphogenesis

ABSTRACT The EH domain proteins Pan1p and End3p of budding yeast have been known to form a complex in vivo and play important roles in organization of the actin cytoskeleton and endocytosis. In this report, we describe new findings concerning the function of the Pan1p-End3p complex. First, we found that the Pan1p-End3p complex associates with Sla1p, another protein known to be required for the assembly of cortical actin structures. Sla1p interacts with the first long repeat region of Pan1p and the N-terminal EH domain of End3p, thus leaving the Pan1p-End3p interaction, which requires the second long repeat of Pan1p and the C-terminal repeat region of End3p, undisturbed. Second, Pan1p, End3p, and Sla1p are also required for normal cell wall morphogenesis. Each of the Pan1-4, sla1Δ, andend3Δ mutants displays the abnormal cell wall morphology previously reported for the act1-1 mutant. These cell wall defects are also exhibited by wild-type cells overproducing the C-terminal region of Sla1p that is responsible for interactions with Pan1p and End3p. These results indicate that the functions of Pan1p, End3p, and Sla1p in cell wall morphogenesis may depend on the formation of a heterotrimeric complex. Interestingly, the cell wall abnormalities exhibited by these cells are independent of the actin cytoskeleton organization on the cell cortex, as they manifest despite the presence of apparently normal cortical actin cytoskeleton. Examination of several act1 mutants also supports this conclusion. These observations suggest that the Pan1p-End3p-Sla1p complex is required not only for normal actin cytoskeleton organization but also for normal cell wall morphogenesis in yeast.

scholarly journals Charge Effects in the Selection of NPF Motifs by the EH Domain of EHD1

Biochemistry ◽  
2010 ◽  
Vol 49 (16) ◽  
pp. 3381-3392 ◽  
Author(s):  
Gillian D. Henry ◽  
Daniel J. Corrigan ◽  
Joseph V. Dineen ◽  
James D. Baleja
Keyword(s):  
Charge Effects ◽  
Eh Domain ◽  
Selection Of

scholarly journals Chemical shift assignments of the C-terminal Eps15 homology domain-3 EH domain

2013 ◽  
Vol 8 (2) ◽  
pp. 263-267
Author(s):  
Gaelle Spagnol ◽  
Calliste Reiling ◽  
Fabien Kieken ◽  
Steve Caplan ◽  
Paul L. Sorgen
Keyword(s):  
Chemical Shift ◽  
Chemical Shift Assignments ◽  
Eh Domain ◽  
Domain 3 ◽  
Eps15 Homology Domain

scholarly journals Thioether-stapled macrocyclic inhibitors of the EH domain of EHD1

2018 ◽  
Vol 26 (6) ◽  
pp. 1206-1211 ◽  
Author(s):  
Alissa J. Kamens ◽  
Kaley M. Mientkiewicz ◽  
Robyn J. Eisert ◽  
Jenna A. Walz ◽  
Charles R. Mace ◽  
...  
Keyword(s):  
Eh Domain

Solution Structure of Eps15's Third EH Domain Reveals Coincident Phe−Trp and Asn−Pro−Phe Binding Sites†,‡

Biochemistry ◽  
2000 ◽  
Vol 39 (15) ◽  
pp. 4309-4319 ◽  
Author(s):  
Jennifer L. Enmon ◽  
Tonny de Beer ◽  
Michael Overduin
Keyword(s):  
Binding Sites ◽  
Solution Structure ◽  
Eh Domain

EHD1—An EH-Domain-Containing Protein with a Specific Expression Pattern

Genomics ◽  
1999 ◽  
Vol 59 (1) ◽  
pp. 66-76 ◽  
Author(s):  
Liat Mintz ◽  
Emilia Galperin ◽  
Metsada Pasmanik-Chor ◽  
Sandra Tulzinsky ◽  
Yael Bromberg ◽  
...  
Keyword(s):  
Expression Pattern ◽  
Specific Expression ◽  
Eh Domain ◽  
Specific Expression Pattern

EH Domain

2002 ◽  
Author(s):  
Tonny de Beer ◽  
Michael Overduin
Keyword(s):  
Eh Domain
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