GGA1
Appearance
ADP-ribosylation factor-binding protein GGA1 is a protein that in humans is encoded by the GGA1 gene.[5][6][7]
Interactions
GGA1 has been shown to interact with Sortilin 1,[8] BACE2,[9] RABEP1[10] and ARF3.[11][12]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000100083 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000033128 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ 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.
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: CS1 maint: unflagged free DOI (link) - ^ 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). Netherlands: 155–8. doi:10.1016/S0014-5793(01)03299-9. ISSN 0014-5793. PMID 11821067.
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(help) - ^ 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). Netherlands: 183–7. doi:10.1016/S0014-5793(02)03052-1. ISSN 0014-5793. PMID 12135764.
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(help) - ^ 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). England: 78–88. doi:10.1093/emboj/cdg015. ISSN 0261-4189. PMC 140067. PMID 12505986.
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(help) - ^ 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). United States: 3078–95. doi:10.1091/mbc.E02-02-0078. ISSN 1059-1524. PMC 124144. PMID 12221117.
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(help) - ^ 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). UNITED STATES: 1241–55. doi:10.1091/mbc.11.4.1241. ISSN 1059-1524. PMC 14844. PMID 10749927.
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