GGA3
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
- ^ a b 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2175099.
- ^ a b 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. PMC 14844. PMID 10749927. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=14844.
- ^ "Entrez Gene: GGA3 golgi associated, gamma adaptin ear containing, ARF binding protein 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23163.
- ^ 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.
- ^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=124144.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2175106.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222692.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=123022.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173151.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=124144.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=140067.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173681.
- 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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PDB gallery
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1jpl: GGA3 VHS domain complexed with C-terminal peptide from cation-independent mannose 6-phosphate receptor
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1juq: GGA3 VHS domain complexed with C-terminal peptide from cation-dependent Mannose 6-phosphate receptor
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1lf8: Complex of GGA3-VHS Domain and CI-MPR C-terminal Phosphopeptide
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1p4u: CRYSTAL STRUCTURE OF GGA3 GAE DOMAIN IN COMPLEX WITH RABAPTIN-5 PEPTIDE
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1wr6: Crystal structure of GGA3 GAT domain in complex with ubiquitin
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1yd8: COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN
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