GGA3

GGA3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesGGA3, golgi associated, gamma adaptin ear containing, ARF binding protein 3
External IDsMGI: 2384159 HomoloGene: 121703 GeneCards: GGA3
Gene location (Human)
Chr.Chromosome 17 (human)[1]
Band17q25.1Start75,236,599 bp[1]
End75,262,363 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

23163

260302

Ensembl

ENSG00000125447

ENSMUSG00000020740

UniProt

Q9NZ52

Q8BMI3

RefSeq (mRNA)

NM_001252067
NM_173048

RefSeq (protein)

NP_001238996
NP_766636

Location (UCSC)Chr 17: 75.24 – 75.26 MbChr 11: 115.58 – 115.6 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

ADP-ribosylation factor-binding protein GGA3 is a protein that in humans is encoded by the GGA3 gene.[5][6]

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.[7]

Interactions

GGA3 has been shown to interact with ARF1[5][8] and ARF3.[6][9]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000125447 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020740 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. 1 2 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.
  6. 1 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.
  7. ↑ "Entrez Gene: GGA3 golgi associated, gamma adaptin ear containing, ARF binding protein 3".
  8. ↑ 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.
  9. ↑ 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. Bibcode:2001Sci...292.1712P. 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. Bibcode:2002Natur.415..933M. 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. Bibcode:2002PNAS...99.8072D. 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. Bibcode:2002Sci...297.1700D. 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. Bibcode:2002PNAS...9916899M. 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.


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