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GGA1

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

ADP-ribosylation factor-binding protein GGA1 is a protein that in humans is encoded by the GGA1 gene.{{cite journal |vauthors=Hirst J, Lui WW, Bright NA, Totty N, Seaman MN, Robinson MS | title = A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome | journal = J Cell Biol | volume = 149 | issue = 1 | pages = 67–80 |date=May 2000 | pmid = 10747088 | pmc = 2175106 | doi =10.1083/jcb.149.1.67 }}{{cite journal |vauthors=Dell'Angelica EC, Puertollano R, Mullins C, Aguilar RC, Vargas JD, Hartnell LM, Bonifacino JS | title = GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex | journal = J Cell Biol | volume = 149 | issue = 1 | pages = 81–94 |date=May 2000 | pmid = 10747089 | pmc = 2175099 | doi =10.1083/jcb.149.1.81 }}{{cite journal |vauthors=Xie L, Boyle D, Sanford D, Scherer PE, Pessin JE, Mora S | title = Intracellular trafficking and secretion of adiponectin is dependent on GGA-coated vesicles | journal = J Biol Chem | volume = 281 | issue = 11 | pages = 7253–9 |date=March 2006 | pmid = 16407204 | doi = 10.1074/jbc.M511313200 | doi-access = free | hdl = 2445/176753 | hdl-access = free }}

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.{{cite web | title = Entrez Gene: GGA1 golgi associated, gamma adaptin ear containing, ARF binding protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26088}}

Interactions

GGA1 has been shown to interact with Sortilin 1,{{cite journal |doi=10.1016/S0014-5793(01)03299-9 |last=Jacobsen |first=Linda |author2=Madsen Peder |author3=Nielsen Morten S |author4=Geraerts Wijnand P M |author5=Gliemann Jørgen |author6=Smit August B |author7=Petersen Claus M |date=January 2002 |title=The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding |journal=FEBS Lett. |volume=511 |issue=1–3 |pages=155–8 | issn = 0014-5793| pmid = 11821067 |s2cid=21977507 |doi-access=free }} BACE2,{{cite journal |last=He |first=Xiangyuan |author2=Chang Wan-Pin |author3=Koelsch Gerald |author4=Tang Jordan |date=July 2002 |title=Memapsin 2 (beta-secretase) cytosolic domain binds to the VHS domains of GGA1 and GGA2: implications on the endocytosis mechanism of memapsin 2 |journal=FEBS Lett. |volume=524 |issue=1–3 |pages=183–7 | issn = 0014-5793| pmid = 12135764 | doi=10.1016/S0014-5793(02)03052-1|doi-access=free }} RABEP1{{cite journal |last=Mattera |first=Rafael |author2=Arighi Cecilia N |author3=Lodge Robert |author4=Zerial Marino |author5=Bonifacino Juan S |date=January 2003 |title=Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex |journal=EMBO J. |volume=22 |issue=1 |pages=78–88 | issn = 0261-4189| pmid = 12505986 |doi = 10.1093/emboj/cdg015 |pmc=140067 }} and ARF3.{{cite journal |last=Boman |first=Annette L |author2=Salo Paul D |author3=Hauglund Melissa J |author4=Strand Nicole L |author5=Rensink Shelly J |author6=Zhdankina Olga |date=September 2002 |title=ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization |journal=Mol. Biol. Cell |volume=13 |issue=9 |pages=3078–95 | issn = 1059-1524| pmid = 12221117 |doi = 10.1091/mbc.E02-02-0078 |pmc=124144 }}{{cite journal |last=Boman |first=A L |author2=Zhang C j |author3=Zhu X |author4=Kahn R A |date=April 2000 |title=A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi |journal=Mol. Biol. Cell |volume=11 |issue=4 |pages=1241–55 | issn = 1059-1524| pmid = 10749927 |pmc=14844 | doi=10.1091/mbc.11.4.1241}}

References

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Further reading

{{refbegin | 2}}

  • {{cite journal |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
  • {{cite journal |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 |display-authors=etal}}
  • {{cite journal |vauthors=Dunham I, Shimizu N, Roe BA |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489–95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031 |display-authors=etal|bibcode=1999Natur.402..489D |doi-access=free }}
  • {{cite journal |vauthors=Boman AL, Zhang C, Zhu X, Kahn RA |title=A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi. |journal=Mol. Biol. Cell |volume=11 |issue= 4 |pages= 1241–55 |year= 2000 |pmid= 10749927 |doi= 10.1091/mbc.11.4.1241| pmc=14844 }}
  • {{cite journal |vauthors=Takatsu H, Yoshino K, Nakayama K |title=Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA proteins that interact with gamma-synergin. |journal=Biochem. Biophys. Res. Commun. |volume=271 |issue= 3 |pages= 719–25 |year= 2000 |pmid= 10814529 |doi= 10.1006/bbrc.2000.2700 }}
  • {{cite journal |vauthors=Zhdankina O, Strand NL, Redmond JM, Boman AL |title=Yeast GGA proteins interact with GTP-bound Arf and facilitate transport through the Golgi. |journal=Yeast |volume=18 |issue= 1 |pages= 1–18 |year= 2001 |pmid= 11124697 |doi= 10.1002/1097-0061(200101)18:1<1::AID-YEA644>3.0.CO;2-5 |s2cid=10348751 |doi-access=free }}
  • {{cite journal |vauthors=Puertollano R, Randazzo PA, Presley JF |title=The GGAs promote ARF-dependent recruitment of clathrin to the TGN. |journal=Cell |volume=105 |issue= 1 |pages= 93–102 |year= 2001 |pmid= 11301005 |doi=10.1016/S0092-8674(01)00299-9 |display-authors=etal|doi-access=free }}
  • {{cite journal |vauthors=Puertollano R, Aguilar RC, Gorshkova I |title=Sorting of mannose 6-phosphate receptors mediated by the GGAs. |journal=Science |volume=292 |issue= 5522 |pages= 1712–6 |year= 2001 |pmid= 11387475 |doi= 10.1126/science.1060750 |display-authors=etal|bibcode=2001Sci...292.1712P |s2cid=30836125 }}
  • {{cite journal |vauthors=Takatsu H, Katoh Y, Shiba Y, Nakayama K |title=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. |journal=J. Biol. Chem. |volume=276 |issue= 30 |pages= 28541–5 |year= 2001 |pmid= 11390366 |doi= 10.1074/jbc.C100218200 |doi-access= free }}
  • {{cite journal |vauthors=Jacobsen L, Madsen P, Nielsen MS |title=The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding. |journal=FEBS Lett. |volume=511 |issue= 1–3 |pages= 155–8 |year= 2002 |pmid= 11821067 |doi=10.1016/S0014-5793(01)03299-9 |s2cid=21977507 |display-authors=etal|doi-access=free }}
  • {{cite journal |vauthors=Shiba T, Takatsu H, Nogi T |title=Structural basis for recognition of acidic-cluster dileucine sequence by GGA1. |journal=Nature |volume=415 |issue= 6874 |pages= 937–41 |year= 2002 |pmid= 11859376 |doi= 10.1038/415937a |display-authors=etal|bibcode=2002Natur.415..937S |s2cid=4395774 }}
  • {{cite journal |vauthors=Takatsu H, Yoshino K, Toda K, Nakayama K |title=GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors. |journal=Biochem. J. |volume=365 |issue= Pt 2 |pages= 369–78 |year= 2002 |pmid= 11950392 |doi= 10.1042/BJ20020428 | pmc=1222692 }}
  • {{cite journal |vauthors=Doray B, Bruns K, Ghosh P, Kornfeld SA |title=Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 12 |pages= 8072–7 |year= 2002 |pmid= 12060753 |doi= 10.1073/pnas.082235699 | pmc=123022 |bibcode=2002PNAS...99.8072D |doi-access=free }}
  • {{cite journal |vauthors=He X, Chang WP, Koelsch G, Tang J |title=Memapsin 2 (beta-secretase) cytosolic domain binds to the VHS domains of GGA1 and GGA2: implications on the endocytosis mechanism of memapsin 2. |journal=FEBS Lett. |volume=524 |issue= 1–3 |pages= 183–7 |year= 2002 |pmid= 12135764 |doi= 10.1016/S0014-5793(02)03052-1|doi-access=free }}
  • {{cite journal |vauthors=Boman AL, Salo PD, Hauglund MJ |title=ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization. |journal=Mol. Biol. Cell |volume=13 |issue= 9 |pages= 3078–95 |year= 2003 |pmid= 12221117 |doi= 10.1091/mbc.E02-02-0078 | pmc=124144 |display-authors=etal}}
  • {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal|bibcode=2002PNAS...9916899M |doi-access=free }}
  • {{cite journal |vauthors=Mattera R, Arighi CN, Lodge R |title=Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex. |journal=EMBO J. |volume=22 |issue= 1 |pages= 78–88 |year= 2003 |pmid= 12505986 |doi= 10.1093/emboj/cdg015 | pmc=140067 |display-authors=etal}}
  • {{cite journal |vauthors=Mills IG, Praefcke GJ, Vallis Y |title=EpsinR: an AP1/clathrin interacting protein involved in vesicle trafficking. |journal=J. Cell Biol. |volume=160 |issue= 2 |pages= 213–22 |year= 2003 |pmid= 12538641 |doi= 10.1083/jcb.200208023 | pmc=2172650 |display-authors=etal}}

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{{PDB Gallery|geneid=26088}}