GGA3

Golgi-associated, gamma adaptin ear containing, ARF binding protein 3
PDB rendering based on 1jpl.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1JPL​, 1JUQ​, 1LF8​, 1P4U​, 1WR6​, 1YD8​
Identifiers
Symbols	GGA3 ; KIAA0154
External IDs	OMIM: 606006 MGI: 2384159 HomoloGene: 121703 GeneCards: GGA3 Gene
Gene ontology Molecular function • protein binding • ADP-ribosylation factor binding Cellular component • trans-Golgi network • endosome membrane • clathrin adaptor complex Biological process • intracellular protein transport • vesicle-mediated transport • positive regulation of protein catabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	23163	260302
Ensembl	ENSG00000125447	ENSMUSG00000020740
UniProt	Q9NZ52	Q8BMI3
RefSeq (mRNA)	NM_001172703	NM_001252067
RefSeq (protein)	NP_001166174	NP_001238996
Location (UCSC)	Chr 17: 75.24 – 75.26 Mb	Chr 11: 115.58 – 115.6 Mb
PubMed search

ADP-ribosylation factor-binding protein GGA3 is a protein that in humans is encoded by the GGA3 gene.^[1][2]

This gene encodes a member of the Golgi-localized, gamma adaptin ear-containing, ARF-binding (GGA) family. This family includes ubiquitous coat proteins that regulate the trafficking of proteins between the trans-Golgi network and the lysosome. These proteins share an amino-terminal VHS domain which mediates sorting of the mannose 6-phosphate receptors at the trans-Golgi network. They also contain a carboxy-terminal region with homology to the ear domain of gamma-adaptins. Alternative splicing of this gene results in two transcript variants.^[3]

Interactions

GGA3 has been shown to interact with ARF1^[1][4] and ARF3.^[5][2]

References

1. Dell'Angelica EC, Puertollano R, Mullins C, Aguilar RC, Vargas JD, Hartnell LM, Bonifacino JS (May 2000). "GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex". J Cell Biol 149 (1): 81–94. doi:10.1083/jcb.149.1.81. PMC 2175099. PMID 10747089.
2. Boman AL, Zhang C, Zhu X, Kahn RA (Jul 2000). "A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi". Mol Biol Cell 11 (4): 1241–55. doi:10.1091/mbc.11.4.1241. PMC 14844. PMID 10749927.
3. "Entrez Gene: GGA3 golgi associated, gamma adaptin ear containing, ARF binding protein 3".
4. Puertollano, R; Randazzo P A; Presley J F; Hartnell L M; Bonifacino J S (Apr 2001). "The GGAs promote ARF-dependent recruitment of clathrin to the TGN". Cell (United States) 105 (1): 93–102. doi:10.1016/S0092-8674(01)00299-9. ISSN 0092-8674. PMID 11301005.
5. Boman, Annette L; Salo Paul D; Hauglund Melissa J; Strand Nicole L; Rensink Shelly J; Zhdankina Olga (Sep 2002). "ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization". Mol. Biol. Cell (United States) 13 (9): 3078–95. doi:10.1091/mbc.E02-02-0078. ISSN 1059-1524. PMC 124144. PMID 12221117.

Further reading

• Nagase T, Seki N, Tanaka A; et al. (1996). "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1.". DNA Res. 2 (4): 167–74, 199–210. doi:10.1093/dnares/2.4.167. PMID 8590280.
• Hirst J, Lui WW, Bright NA; et al. (2000). "A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome.". J. Cell Biol. 149 (1): 67–80. doi:10.1083/jcb.149.1.67. PMC 2175106. PMID 10747088.
• Takatsu H, Yoshino K, Nakayama K (2000). "Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA proteins that interact with gamma-synergin.". Biochem. Biophys. Res. Commun. 271 (3): 719–25. doi:10.1006/bbrc.2000.2700. PMID 10814529.
• Puertollano R, Randazzo PA, Presley JF; et al. (2001). "The GGAs promote ARF-dependent recruitment of clathrin to the TGN.". Cell 105 (1): 93–102. doi:10.1016/S0092-8674(01)00299-9. PMID 11301005.
• Puertollano R, Aguilar RC, Gorshkova I; et al. (2001). "Sorting of mannose 6-phosphate receptors mediated by the GGAs.". Science 292 (5522): 1712–6. doi:10.1126/science.1060750. PMID 11387475.
• Misra S, Puertollano R, Kato Y; et al. (2002). "Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains.". Nature 415 (6874): 933–7. doi:10.1038/415933a. PMID 11859375.
• Takatsu H, Yoshino K, Toda K, Nakayama K (2002). "GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors.". Biochem. J. 365 (Pt 2): 369–78. doi:10.1042/BJ20020428. PMC 1222692. PMID 11950392.
• Kato Y, Misra S, Puertollano R; et al. (2002). "Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism.". Nat. Struct. Biol. 9 (7): 532–6. doi:10.1038/nsb807. PMID 12032548.
• Doray B, Bruns K, Ghosh P, Kornfeld SA (2002). "Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif.". Proc. Natl. Acad. Sci. U.S.A. 99 (12): 8072–7. doi:10.1073/pnas.082235699. PMC 123022. PMID 12060753.
• Wasiak S, Legendre-Guillemin V, Puertollano R; et al. (2002). "Enthoprotin: a novel clathrin-associated protein identified through subcellular proteomics.". J. Cell Biol. 158 (5): 855–62. doi:10.1083/jcb.200205078. PMC 2173151. PMID 12213833.
• Doray B, Ghosh P, Griffith J; et al. (2002). "Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network.". Science 297 (5587): 1700–3. doi:10.1126/science.1075327. PMID 12215646.
• Boman AL, Salo PD, Hauglund MJ; et al. (2003). "ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization.". Mol. Biol. Cell 13 (9): 3078–95. doi:10.1091/mbc.E02-02-0078. PMC 124144. PMID 12221117.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Mattera R, Arighi CN, Lodge R; et al. (2003). "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex.". EMBO J. 22 (1): 78–88. doi:10.1093/emboj/cdg015. PMC 140067. PMID 12505986.
• Wakasugi M, Waguri S, Kametaka S; et al. (2003). "Predominant expression of the short form of GGA3 in human cell lines and tissues.". Biochem. Biophys. Res. Commun. 306 (3): 687–92. doi:10.1016/S0006-291X(03)01032-5. PMID 12810073.
• He X, Zhu G, Koelsch G; et al. (2003). "Biochemical and structural characterization of the interaction of memapsin 2 (beta-secretase) cytosolic domain with the VHS domain of GGA proteins.". Biochemistry 42 (42): 12174–80. doi:10.1021/bi035199h. PMID 14567678.
• Ghosh P, Griffith J, Geuze HJ, Kornfeld S (2004). "Mammalian GGAs act together to sort mannose 6-phosphate receptors.". J. Cell Biol. 163 (4): 755–66. doi:10.1083/jcb.200308038. PMC 2173681. PMID 14638859.
• Shiba Y, Katoh Y, Shiba T; et al. (2004). "GAT (GGA and Tom1) domain responsible for ubiquitin binding and ubiquitination.". J. Biol. Chem. 279 (8): 7105–11. doi:10.1074/jbc.M311702200. PMID 14660606.