PDBsum entry 1gyu

Endocytosis

PDB id

1gyu

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Contents

			Protein chain

					120 a.a. *

			Waters ×171

* Residue conservation analysis

PDB id:

1gyu

Links

Name:

Endocytosis

Title:

Gamma-adaptin appendage domain from clathrin adaptor ap1

Structure:

Adapter-related protein complex 1 gamma 1 subunit. Chain: a. Fragment: appendage domain, residues 703-821. Synonym: gamma-adaptin, golgi adaptor ha1/ap1 adaptin gamma subunit, clathrin assembly protein complex 1 gamma large chain. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.81Å

R-factor:

0.180

R-free:

0.223

Authors:

P.R.Evans,D.J.Owen,H.M.Mcmahon,H.M.Kent

Key ref:

H.M.Kent et al. (2002). Gamma-adaptin appendage domain: structure and binding site for Eps15 and gamma-synergin. Structure, 10, 1139-1148. PubMed id: 12176391 DOI: 10.1016/S0969-2126(02)00801-8

Date:

30-Apr-02

Release date:

22-Aug-02

PROCHECK

	Headers

	References

Protein chain

P22892 (AP1G1_MOUSE) - AP-1 complex subunit gamma-1 from Mus musculus

Seq: Struc:

Seq: Struc:					822 a.a. 120 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1016/S0969-2126(02)00801-8	Structure 10:1139-1148 (2002)
PubMed id: 12176391

Gamma-adaptin appendage domain: structure and binding site for Eps15 and gamma-synergin.
H.M.Kent, H.T.McMahon, P.R.Evans, A.Benmerah, D.J.Owen.

ABSTRACT

The AP1 complex is one of a family of heterotetrameric clathrin-adaptor complexes involved in vesicular trafficking between the Golgi and endosomes. The complex has two large subunits, gamma and beta1, which can be divided into trunk, hinge, and appendage domains. The 1.8 A resolution structure of the gamma appendage is presented. The binding site for the known gamma appendage ligand gamma-synergin is mapped through creation of point mutations designed on the basis of the structure. We also show that Eps15, a protein believed to be involved in vesicle formation at the plasma membrane, is also a ligand of gamma appendage and binds to the same site as gamma-synergin. This observation explains the demonstrated brefeldinA (BFA)-sensitive colocalization of Eps15 and AP1 at the Golgi complex.

Selected figure(s)



	Figure 1. Figure 1. Comparison of the Structures of the g and a Appendages(A) Superposition of the Ca traces of g appendage (purple) and a appendage N-terminal subdomain (green). The two overlay with an rms deviation of 1.8 � for 96 Ca atoms.(B) Schematic representation of the g appendage domain. Point mutations that abrogate binding to g-synergin and Eps15 are shown in yellow in ball and stick representation. All protein structure pictures were made using Aesop (M.E.M. Noble, personal communication).(C) Schematic representation of the a appendage domain. The N-terminal subdomain is in green and the C-terminal subdomain in gold.(D) Structure-based sequence alignment of g appendages from human, mouse, Arabidopsis, and smutfungus, mouse g2-appendage, human GGA1 appendage, and the N-terminal subdomain of the a appendage. The positions of b strands are marked by arrows and a helices with rods (purple human g appendage and green a appendage). Conserved residues are indicated by gray shading and residues identical between the g and a appendages are marked with an asterisk.(E) Ca trace of the g appendage in stereo representation.

Figure was selected by an automated process.

Literature references that cite this PDB file's key reference

PubMed id

Reference

19054391

N.Rismanchi, R.Puertollano, and C.Blackstone (2009).
STAM Adaptor Proteins Interact with COPII Complexes and Function in ER-to-Golgi Trafficking.

Traffic, 10, 201-217.

19814798

P.M.van Bergen En Henegouwen (2009).
Eps15: a multifunctional adaptor protein regulating intracellular trafficking.

Cell Commun Signal, 7, 24.

18211691

C.J.DeRegis, P.B.Rahl, G.R.Hoffman, R.A.Cerione, and R.N.Collins (2008).
Mutational analysis of betaCOP (Sec26p) identifies an appendage domain critical for function.

BMC Cell Biol, 9, 3.

17988225

G.R.Medigeshi, M.Krikunova, K.Radhakrishnan, D.Wenzel, J.Klingauf, and P.Schu (2008).
AP-1 Membrane-Cytoplasm Recycling Regulated by mu1A-Adaptin.

Traffic, 9, 121-132.

18843039

P.A.Keyel, J.R.Thieman, R.Roth, E.Erkan, E.T.Everett, S.C.Watkins, J.E.Heuser, and L.M.Traub (2008).
The AP-2 adaptor beta2 appendage scaffolds alternate cargo endocytosis.

Mol Biol Cell, 19, 5309-5326.

18524853

S.Chi, H.Cao, J.Chen, and M.A.McNiven (2008).
Eps15 mediates vesicle trafficking from the trans-Golgi network via an interaction with the clathrin adaptor AP-1.

Mol Biol Cell, 19, 3564-3575.

17762867

B.Ritter, A.Y.Denisov, J.Philie, P.D.Allaire, V.Legendre-Guillemin, P.Zylbergold, K.Gehring, and P.S.McPherson (2007).
The NECAP PHear domain increases clathrin accessory protein binding potential.

EMBO J, 26, 4066-4077.

17596511

G.A.Mardones, P.V.Burgos, D.A.Brooks, E.Parkinson-Lawrence, R.Mattera, and J.S.Bonifacino (2007).
The trans-Golgi network accessory protein p56 promotes long-range movement of GGA/clathrin-containing transport carriers and lysosomal enzyme sorting.

Mol Biol Cell, 18, 3486-3501.

17692542

I.G.Mills (2007).
The interplay between clathrin-coated vesicles and cell signalling.

Semin Cell Dev Biol, 18, 459-470.

17506864

M.Inoue, T.Shiba, K.Ihara, Y.Yamada, S.Hirano, H.Kamikubo, M.Kataoka, M.Kawasaki, R.Kato, K.Nakayama, and S.Wakatsuki (2007).
Molecular basis for autoregulatory interaction between GAE domain and hinge region of GGA1.

Traffic, 8, 904-913.

PDB codes:

2dwx 2dwy

17538018

S.Kametaka, K.Moriyama, P.V.Burgos, E.Eisenberg, L.E.Greene, R.Mattera, and J.S.Bonifacino (2007).
Canonical interaction of cyclin G associated kinase with adaptor protein 1 regulates lysosomal enzyme sorting.

Mol Biol Cell, 18, 2991-3001.

17052248

C.Knuehl, C.Y.Chen, V.Manalo, P.K.Hwang, N.Ota, and F.M.Brodsky (2006).
Novel binding sites on clathrin and adaptors regulate distinct aspects of coat assembly.

Traffic, 7, 1688-1700.

16903783

E.M.Schmid, M.G.Ford, A.Burtey, G.J.Praefcke, S.Y.Peak-Chew, I.G.Mills, A.Benmerah, and H.T.McMahon (2006).
Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly.

PLoS Biol, 4, e262.

PDB codes:

2iv8 2iv9

16493411

M.A.Edeling, C.Smith, and D.Owen (2006).
Life of a clathrin coat: insights from clathrin and AP structures.

Nat Rev Mol Cell Biol, 7, 32-44.

16973870

M.A.McNiven, and H.M.Thompson (2006).
Vesicle formation at the plasma membrane and trans-Golgi network: the same but different.

Science, 313, 1591-1594.

15516337

C.C.Wreden, M.Wlizla, and R.J.Reimer (2005).
Varied mechanisms underlie the free sialic acid storage disorders.

J Biol Chem, 280, 1408-1416.

16131760

C.Mueller-Dieckmann, S.Panjikar, P.A.Tucker, and M.S.Weiss (2005).
On the routine use of soft X-rays in macromolecular crystallography. Part III. The optimal data-collection wavelength.

Acta Crystallogr D Biol Crystallogr, 61, 1263-1272.

PDB codes:

2a7a 2a7b 2a7c 2a7d 2a7e 2a7f 2a7g 2a7h 2a7i 2a7j

15758025

J.Hirst, G.H.Borner, M.Harbour, and M.S.Robinson (2005).
The aftiphilin/p200/gamma-synergin complex.

Mol Biol Cell, 16, 2554-2565.

15775984

V.E.Neubrand, R.D.Will, W.Möbius, A.Poustka, S.Wiemann, P.Schu, C.G.Dotti, R.Pepperkok, and J.C.Simpson (2005).
Gamma-BAR, a novel AP-1-interacting protein involved in post-Golgi trafficking.

EMBO J, 24, 1122-1133.

15930630

Y.Yamada, M.Inoue, T.Shiba, M.Kawasaki, R.Kato, K.Nakayama, and S.Wakatsuki (2005).
Structure determination of GGA-GAE and gamma1-ear in complex with peptides: crystallization of low-affinity complexes in membrane traffic.

Acta Crystallogr D Biol Crystallogr, 61, 731-736.

14565955

A.Jha, N.R.Agostinelli, S.K.Mishra, P.A.Keyel, M.J.Hawryluk, and L.M.Traub (2004).
A novel AP-2 adaptor interaction motif initially identified in the long-splice isoform of synaptojanin 1, SJ170.

J Biol Chem, 279, 2281-2290.

15359277

B.Ritter, A.Y.Denisov, J.Philie, C.Deprez, E.C.Tung, K.Gehring, and P.S.McPherson (2004).
Two WXXF-based motifs in NECAPs define the specificity of accessory protein binding to AP-1 and AP-2.

EMBO J, 23, 3701-3710.

15473838

D.J.Owen, B.M.Collins, and P.R.Evans (2004).
Adaptors for clathrin coats: structure and function.

Annu Rev Cell Dev Biol, 20, 153-191.

14973137

H.Bai, B.Doray, and S.Kornfeld (2004).
GGA1 interacts with the adaptor protein AP-1 through a WNSF sequence in its hinge region.

J Biol Chem, 279, 17411-17417.

15261670

H.T.McMahon, and I.G.Mills (2004).
COP and clathrin-coated vesicle budding: different pathways, common approaches.

Curr Opin Cell Biol, 16, 379-391.

14708007

J.S.Bonifacino (2004).
The GGA proteins: adaptors on the move.

Nat Rev Mol Cell Biol, 5, 23-32.

14690497

P.J.Watson, G.Frigerio, B.M.Collins, R.Duden, and D.J.Owen (2004).
Gamma-COP appendage domain - structure and function.

Traffic, 5, 79-88.

PDB code:

1r4x

14665628

R.Mattera, B.Ritter, S.S.Sidhu, P.S.McPherson, and J.S.Bonifacino (2004).
Definition of the consensus motif recognized by gamma-adaptin ear domains.

J Biol Chem, 279, 8018-8028.

15292237

S.K.Mishra, M.J.Hawryluk, T.J.Brett, P.A.Keyel, A.L.Dupin, A.Jha, J.E.Heuser, D.H.Fremont, and L.M.Traub (2004).
Dual engagement regulation of protein interactions with the AP-2 adaptor alpha appendage.

J Biol Chem, 279, 46191-46203.

12858163

B.M.Collins, G.J.Praefcke, M.S.Robinson, and D.J.Owen (2003).
Structural basis for binding of accessory proteins by the appendage domain of GGAs.

Nat Struct Biol, 10, 607-613.

PDB code:

1om9

12886287

C.Knuehl, and F.M.Brodsky (2003).
The long and short of adaptor appendages.

Nat Struct Biol, 10, 580-582.

14573946

G.Evans, and G.Bricogne (2003).
Triiodide derivatization in protein crystallography.

Acta Crystallogr D Biol Crystallogr, 59, 1923-1929.

12858162

G.J.Miller, R.Mattera, J.S.Bonifacino, and J.H.Hurley (2003).
Recognition of accessory protein motifs by the gamma-adaptin ear domain of GGA3.

Nat Struct Biol, 10, 599-606.

PDB code:

1p4u

14527408

G.R.Hoffman, P.B.Rahl, R.N.Collins, and R.A.Cerione (2003).
Conserved structural motifs in intracellular trafficking pathways: structure of the gammaCOP appendage domain.

Mol Cell, 12, 615-625.

PDB code:

1pzd

12538641

I.G.Mills, G.J.Praefcke, Y.Vallis, B.J.Peter, L.E.Olesen, J.L.Gallop, P.J.Butler, P.R.Evans, and H.T.McMahon (2003).
EpsinR: an AP1/clathrin interacting protein involved in vesicle trafficking.

J Cell Biol, 160, 213-222.

12589059

J.Hirst, A.Motley, K.Harasaki, S.Y.Peak Chew, and M.S.Robinson (2003).
EpsinR: an ENTH domain-containing protein that interacts with AP-1.

Mol Biol Cell, 14, 625-641.

14745135

K.Nakayama, and S.Wakatsuki (2003).
The structure and function of GGAs, the traffic controllers at the TGN sorting crossroads.

Cell Struct Funct, 28, 431-442.

12483220

M.C.Duncan, G.Costaguta, and G.S.Payne (2003).
Yeast epsin-related proteins required for Golgi-endosome traffic define a gamma-adaptin ear-binding motif.

Nat Cell Biol, 5, 77-81.

12742163

M.C.Duncan, and G.S.Payne (2003).
ENTH/ANTH domains expand to the Golgi.

Trends Cell Biol, 13, 211-215.

12773381

M.Deneka, M.Neeft, I.Popa, M.van Oort, H.Sprong, V.Oorschot, J.Klumperman, P.Schu, and P.van der Sluijs (2003).
Rabaptin-5alpha/rabaptin-4 serves as a linker between rab4 and gamma(1)-adaptin in membrane recycling from endosomes.

EMBO J, 22, 2645-2657.

12505986

R.Mattera, C.N.Arighi, R.Lodge, M.Zerial, and J.S.Bonifacino (2003).
Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex.

EMBO J, 22, 78-88.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.