Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 687-700 |
| Number of pages | 14 |
| Journal | Molecular Biology of the Cell |
| Volume | 23 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 2012 Feb 15 |
Fingerprint
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology
Cite this
Regulation of clathrin coat assembly by Eps15 homology domain-mediated interactions during endocytosis. / Suzuki, Ryohei; Toshima, Junko Y.; Toshima, Jiro.
In: Molecular Biology of the Cell, Vol. 23, No. 4, 15.02.2012, p. 687-700.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Regulation of clathrin coat assembly by Eps15 homology domain-mediated interactions during endocytosis
AU - Suzuki, Ryohei
AU - Toshima, Junko Y.
AU - Toshima, Jiro
PY - 2012/2/15
Y1 - 2012/2/15
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84857206318&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84857206318&partnerID=8YFLogxK
U2 - 10.1091/mbc.E11-04-0380
DO - 10.1091/mbc.E11-04-0380
M3 - Article
C2 - 22190739
AN - SCOPUS:84857206318
VL - 23
SP - 687
EP - 700
JO - Molecular Biology of the Cell
JF - Molecular Biology of the Cell
SN - 1059-1524
IS - 4
ER -