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Gamma-synergin: an EH domain-containing protein that interacts with gamma-adaptin.

Page LJ, Sowerby PJ, Lui WW, Robinson MS - J. Cell Biol. (1999)

Bottom Line: It binds directly to the ear domain of gamma-adaptin and it contains an Eps15 homology (EH) domain, although the EH domain is not part of the gamma-adaptin binding site.In cells expressing alpha-adaptin with the gamma-adaptin ear, a construct that goes mainly to the plasma membrane, much of the gamma-synergin is also rerouted to the plasma membrane, indicating that it follows AP-1 onto membranes rather than leading it there.The presence of an EH domain suggests that gamma-synergin links the AP-1 complex to another protein or proteins.

View Article: PubMed Central - PubMed

Affiliation: Department of Clinical Biochemistry and Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 2XY, England.

ABSTRACT
The AP-1 adaptor complex is associated with the TGN, where it links selected membrane proteins to the clathrin lattice, enabling these proteins to be concentrated in clathrin-coated vesicles. To identify other proteins that participate in the clathrin-coated vesicle cycle at the TGN, we have carried out a yeast two- hybrid library screen using the gamma-adaptin subunit of the AP-1 complex as bait. Two novel, ubiquitously expressed proteins were found: p34, which interacts with both gamma-adaptin and alpha-adaptin, and gamma-synergin, an alternatively spliced protein with an apparent molecular mass of approximately 110-190 kD, which only interacts with gamma-adaptin. gamma-Synergin is associated with AP-1 both in the cytosol and on TGN membranes, and it is strongly enriched in clathrin-coated vesicles. It binds directly to the ear domain of gamma-adaptin and it contains an Eps15 homology (EH) domain, although the EH domain is not part of the gamma-adaptin binding site. In cells expressing alpha-adaptin with the gamma-adaptin ear, a construct that goes mainly to the plasma membrane, much of the gamma-synergin is also rerouted to the plasma membrane, indicating that it follows AP-1 onto membranes rather than leading it there. The presence of an EH domain suggests that gamma-synergin links the AP-1 complex to another protein or proteins.

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Characteristics of γ-synergin. (a) The schematic diagram shows the positions of the alternative splice sites (AS), EH domain, γ-adaptin–binding domain, and DDFD/EXF sequences (D). (b) Comparison of the EH domain of γ-synergin with that of several well characterized EH domain-containing proteins: the mammalian proteins Eps15 and Ese1, and the yeast proteins Pan1p and End3p.
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Figure 3: Characteristics of γ-synergin. (a) The schematic diagram shows the positions of the alternative splice sites (AS), EH domain, γ-adaptin–binding domain, and DDFD/EXF sequences (D). (b) Comparison of the EH domain of γ-synergin with that of several well characterized EH domain-containing proteins: the mammalian proteins Eps15 and Ese1, and the yeast proteins Pan1p and End3p.

Mentions: A schematic diagram of γ-synergin is shown in Fig. 3 a, indicating the positions of the EH domain, some of the alternative splice sites, and the γ-adaptin–binding domain (see below). Fig. 3 b shows an alignment of the EH domains from γ-synergin, Eps15, Ese1, End3p, and Pan1p. The EH domain of γ-synergin can be seen to contain all of the highly conserved amino acids found in other, well characterized EH domains. However, apart from the EH domain, γ-synergin shows no significant sequence homology to any other proteins in the database, and it does not share any of the other features found in the α-adaptin binding partner Eps15 such as a coiled-coil domain or a proline-rich region.


Gamma-synergin: an EH domain-containing protein that interacts with gamma-adaptin.

Page LJ, Sowerby PJ, Lui WW, Robinson MS - J. Cell Biol. (1999)

Characteristics of γ-synergin. (a) The schematic diagram shows the positions of the alternative splice sites (AS), EH domain, γ-adaptin–binding domain, and DDFD/EXF sequences (D). (b) Comparison of the EH domain of γ-synergin with that of several well characterized EH domain-containing proteins: the mammalian proteins Eps15 and Ese1, and the yeast proteins Pan1p and End3p.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2169493&req=5

Figure 3: Characteristics of γ-synergin. (a) The schematic diagram shows the positions of the alternative splice sites (AS), EH domain, γ-adaptin–binding domain, and DDFD/EXF sequences (D). (b) Comparison of the EH domain of γ-synergin with that of several well characterized EH domain-containing proteins: the mammalian proteins Eps15 and Ese1, and the yeast proteins Pan1p and End3p.
Mentions: A schematic diagram of γ-synergin is shown in Fig. 3 a, indicating the positions of the EH domain, some of the alternative splice sites, and the γ-adaptin–binding domain (see below). Fig. 3 b shows an alignment of the EH domains from γ-synergin, Eps15, Ese1, End3p, and Pan1p. The EH domain of γ-synergin can be seen to contain all of the highly conserved amino acids found in other, well characterized EH domains. However, apart from the EH domain, γ-synergin shows no significant sequence homology to any other proteins in the database, and it does not share any of the other features found in the α-adaptin binding partner Eps15 such as a coiled-coil domain or a proline-rich region.

Bottom Line: It binds directly to the ear domain of gamma-adaptin and it contains an Eps15 homology (EH) domain, although the EH domain is not part of the gamma-adaptin binding site.In cells expressing alpha-adaptin with the gamma-adaptin ear, a construct that goes mainly to the plasma membrane, much of the gamma-synergin is also rerouted to the plasma membrane, indicating that it follows AP-1 onto membranes rather than leading it there.The presence of an EH domain suggests that gamma-synergin links the AP-1 complex to another protein or proteins.

View Article: PubMed Central - PubMed

Affiliation: Department of Clinical Biochemistry and Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 2XY, England.

ABSTRACT
The AP-1 adaptor complex is associated with the TGN, where it links selected membrane proteins to the clathrin lattice, enabling these proteins to be concentrated in clathrin-coated vesicles. To identify other proteins that participate in the clathrin-coated vesicle cycle at the TGN, we have carried out a yeast two- hybrid library screen using the gamma-adaptin subunit of the AP-1 complex as bait. Two novel, ubiquitously expressed proteins were found: p34, which interacts with both gamma-adaptin and alpha-adaptin, and gamma-synergin, an alternatively spliced protein with an apparent molecular mass of approximately 110-190 kD, which only interacts with gamma-adaptin. gamma-Synergin is associated with AP-1 both in the cytosol and on TGN membranes, and it is strongly enriched in clathrin-coated vesicles. It binds directly to the ear domain of gamma-adaptin and it contains an Eps15 homology (EH) domain, although the EH domain is not part of the gamma-adaptin binding site. In cells expressing alpha-adaptin with the gamma-adaptin ear, a construct that goes mainly to the plasma membrane, much of the gamma-synergin is also rerouted to the plasma membrane, indicating that it follows AP-1 onto membranes rather than leading it there. The presence of an EH domain suggests that gamma-synergin links the AP-1 complex to another protein or proteins.

Show MeSH
Related in: MedlinePlus