GGA1

ADP-ribosylation factor-binding protein GGA1 is a protein that in humans is encoded by the GGA1 gene.[5][6][7]

GGA1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesGGA1, golgi associated, gamma adaptin ear containing, ARF binding protein 1
External IDsOMIM: 606004 MGI: 2146207 HomoloGene: 39250 GeneCards: GGA1
Orthologs
SpeciesHumanMouse
Entrez

26088

106039

Ensembl

ENSG00000100083

ENSMUSG00000033128

UniProt

Q9UJY5

Q8R0H9

RefSeq (mRNA)

NM_145929

RefSeq (protein)

NP_001001560
NP_001166158
NP_001166159
NP_037497
NP_001350700

NP_666041

Location (UCSC)Chr 22: 37.61 – 37.63 MbChr 15: 78.76 – 78.78 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[8]

Interactions

GGA1 has been shown to interact with Sortilin 1,[9] BACE2,[10] RABEP1[11] and ARF3.[12][13]

References

  1. GRCh38: Ensembl release 89: ENSG00000100083 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000033128 - 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. 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.
  6. 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.
  7. 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.
  8. "Entrez Gene: GGA1 golgi associated, gamma adaptin ear containing, ARF binding protein 1".
  9. 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. S2CID 21977507.
  10. 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.
  11. 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.
  12. 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.
  13. 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

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