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GGA1
Introduction
ADP-ribosylation factor-binding protein GGA1 is a protein that in humans is encoded by the GGA1 gene.[1][2][3]
This gene encodes a member of the Golgi-localized, gamma adaptin ear-containing, ARF-binding (GGA) protein family. Members of this family are 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. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.[4]
Interactions
Interactions
GGA1 has been shown to interact with Sortilin 1,[5] BACE2,[6] RABEP1[7] and ARF3.[8][9]
References
References
- ↑ Hirst J, Lui WW, Bright NA, Totty N, Seaman MN, Robinson MS (May 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.
- ↑ 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.
- ↑ Xie L, Boyle D, Sanford D, Scherer PE, Pessin JE, Mora S (March 2006). “Intracellular trafficking and secretion of adiponectin is dependent on GGA-coated vesicles”. J Biol Chem. 281 (11): 7253–9. doi:10.1074/jbc.M511313200. PMID 16407204.
- ↑ “Entrez Gene: GGA1 golgi associated, gamma adaptin ear containing, ARF binding protein 1”.
- ↑ Jacobsen, Linda; Madsen Peder; Nielsen Morten S; Geraerts Wijnand P M; Gliemann Jørgen; Smit August B; Petersen Claus M (January 2002). “The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding”. FEBS Lett. 511 (1–3): 155–8. doi:10.1016/S0014-5793(01)03299-9. ISSN 0014-5793. PMID 11821067.
- ↑ He, Xiangyuan; Chang Wan-Pin; Koelsch Gerald; Tang Jordan (July 2002). “Memapsin 2 (beta-secretase) cytosolic domain binds to the VHS domains of GGA1 and GGA2: implications on the endocytosis mechanism of memapsin 2”. FEBS Lett. 524 (1–3): 183–7. doi:10.1016/S0014-5793(02)03052-1. ISSN 0014-5793. PMID 12135764.
- ↑ Mattera, Rafael; Arighi Cecilia N; Lodge Robert; Zerial Marino; Bonifacino Juan S (January 2003). “Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex”. EMBO J. 22 (1): 78–88. doi:10.1093/emboj/cdg015. ISSN 0261-4189. PMC 140067. PMID 12505986.
- ↑ Boman, Annette L; Salo Paul D; Hauglund Melissa J; Strand Nicole L; Rensink Shelly J; Zhdankina Olga (September 2002). “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. ISSN 1059-1524. PMC 124144. PMID 12221117.
- ↑ Boman, A L; Zhang C j; Zhu X; Kahn R A (April 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. ISSN 1059-1524. PMC 14844. PMID 10749927.
Further reading
Further reading
- Maruyama K, Sugano S (1994). “Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides”. Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). “Construction and characterization of a full length-enriched and a 5′-end-enriched cDNA library”. Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Dunham I, Shimizu N, Roe BA, et al. (1999). “The DNA sequence of human chromosome 22”. Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.
- Boman AL, Zhang C, Zhu X, Kahn RA (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.
- 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.
- Zhdankina O, Strand NL, Redmond JM, Boman AL (2001). “Yeast GGA proteins interact with GTP-bound Arf and facilitate transport through the Golgi”. Yeast. 18 (1): 1–18. doi:10.1002/1097-0061(200101)18:1<1::AID-YEA644>3.0.CO;2-5. PMID 11124697.
- 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.
- Takatsu H, Katoh Y, Shiba Y, Nakayama K (2001). “Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains”. J. Biol. Chem. 276 (30): 28541–5. doi:10.1074/jbc.C100218200. PMID 11390366.
- Jacobsen L, Madsen P, Nielsen MS, et al. (2002). “The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding”. FEBS Lett. 511 (1–3): 155–8. doi:10.1016/S0014-5793(01)03299-9. PMID 11821067.
- Shiba T, Takatsu H, Nogi T, et al. (2002). “Structural basis for recognition of acidic-cluster dileucine sequence by GGA1”. Nature. 415 (6874): 937–41. Bibcode:2002Natur.415..937S. doi:10.1038/415937a. PMID 11859376.
- 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.
- 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.
- He X, Chang WP, Koelsch G, Tang J (2002). “Memapsin 2 (beta-secretase) cytosolic domain binds to the VHS domains of GGA1 and GGA2: implications on the endocytosis mechanism of memapsin 2”. FEBS Lett. 524 (1–3): 183–7. doi:10.1016/S0014-5793(02)03052-1. PMID 12135764.
- 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.
- Mills IG, Praefcke GJ, Vallis Y, et al. (2003). “EpsinR: an AP1/clathrin interacting protein involved in vesicle trafficking”. J. Cell Biol. 160 (2): 213–22. doi:10.1083/jcb.200208023. PMC 2172650. PMID 12538641.