GGA3 – Wikipedia

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Protein-coding gene in the species Homo sapiens

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[edit]

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

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000125447 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020740 – Ensembl, May 2017
  3. ^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Dell’Angelica EC, Puertollano R, Mullins C, Aguilar RC, Vargas JD, Hartnell LM, Bonifacino JS (April 2000). “GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex”. The Journal of Cell Biology. 149 (1): 81–94. doi:10.1083/jcb.149.1.81. PMC 2175099. PMID 10747089.
  6. ^ a b Boman AL, Zhang C, Zhu X, Kahn RA (April 2000). “A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi”. Molecular Biology of the 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 PA, Presley JF, Hartnell LM, Bonifacino JS (April 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. S2CID 1158816.
  9. ^ Boman AL, Salo PD, Hauglund MJ, Strand NL, Rensink SJ, Zhdankina O (September 2002). “ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization”. Molecular Biology of the Cell. 13 (9): 3078–95. doi:10.1091/mbc.E02-02-0078. PMC 124144. PMID 12221117.

Further reading[edit]