GGA1

GGA1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1J2J, 1JWF, 1JWG, 1NA8, 1NAF, 1NWM, 1O3X, 1OM9, 1OXZ, 1PY1, 1UJJ, 1UJK, 1X79, 2DWX, 2DWY, 3G2S, 3G2T, 3G2U, 3G2V, 3G2W Contents Interactions ; References ; Further reading ;
Identifiers
Aliases	GGA1 , golgi associated, gamma adaptin ear containing, ARF binding protein 1
External IDs	OMIM: 606004 MGI: 2146207 HomoloGene: 39250 GeneCards: GGA1
Gene location (Human)
Chr.	Chromosome 22 (human)
End	37,633,564 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	78,778,785 bp
RNA expression pattern
	Top expressed in
	pancreatic ductal cell; ; endothelial cell; ; right uterine tube; ; pituitary gland; ; anterior pituitary; ; right lobe of thyroid gland; ; tibialis anterior muscle; ; left lobe of thyroid gland; ; spleen; ; parotid gland;
	Top expressed in
	lip; ; pyloric antrum; ; yolk sac; ; superior frontal gyrus; ; esophagus; ; cerebellar cortex; ; internal carotid artery; ; spermatocyte; ; duodenum; ; crypt of lieberkuhn of small intestine;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	protein binding ; protein heterodimerization activity ; molecular function ;
Cellular component	endosome ; Golgi apparatus ; endosome membrane ; intracellular anatomical structure ; membrane ; intracellular membrane-bounded organelle ; clathrin adaptor complex ; nucleoplasm ; early endosome membrane ; early endosome ; cytosol ; protein-containing complex ;
Biological process	protein transport ; intracellular protein transport ; toxin transport ; positive regulation of protein catabolic process ; vesicle-mediated transport ; transport ; Golgi to plasma membrane transport ; protein localization ; protein localization to cell surface ; retrograde transport, endosome to Golgi ; Golgi to plasma membrane protein transport ; protein localization to ciliary membrane ;
	Sources:Amigo / QuickGO
Orthologs
	26088
	106039
	ENSG00000100083
	ENSMUSG00000033128
	Q9UJY5
	Q8R0H9
NM_001001560 ; NM_001001561 ; NM_001172687 ; NM_001172688 ; NM_013365 ;
	NM_001363771
	NM_145929
	NP_001001560 ; NP_001166158 ; NP_001166159 ; NP_037497 ; NP_001350700
	NP_666041
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated January 05, 2024

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

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]

Related Research Articles

COPI is a coatomer, a protein complex that coats vesicles transporting proteins from the cis end of the Golgi complex back to the rough endoplasmic reticulum (ER), where they were originally synthesized, and between Golgi compartments. This type of transport is retrograde transport, in contrast to the anterograde transport associated with the COPII protein. The name "COPI" refers to the specific coat protein complex that initiates the budding process on the cis-Golgi membrane. The coat consists of large protein subcomplexes that are made of seven different protein subunits, namely α, β, β', γ, δ, ε and ζ.

ADP-ribosylation factor 6 (ARF6) is a member of the ADP ribosylation factor family of GTP-binding proteins. ARF6 has a variety of cellular functions that are frequently involved in trafficking of biological membranes and transmembrane protein cargo. ARF6 has specifically been implicated in endocytosis of plasma membrane proteins and also, to a lesser extent, plasma membrane protein recycling.

ADP-ribosylation factor 1 is a protein that in humans is encoded by the ARF1 gene.

Coatomer subunit beta is a protein that in humans is encoded by the COPB1 gene.

ADP-ribosylation factor-binding protein GGA3 is a protein that in humans is encoded by the GGA3 gene.

AP-1 complex subunit gamma-1 is a protein that in humans is encoded by the AP1G1 gene.

ADP-ribosylation factor-binding protein GGA2 is a protein that in humans is encoded by the GGA2 gene.

AP-1 complex subunit beta-1 is a protein that in humans is encoded by the AP1B1 gene.

ADP-ribosylation factor 3 is a protein that in humans is encoded by the ARF3 gene.

AP-1 complex subunit sigma-1A is a protein that in humans is encoded by the AP1S1 gene.

Golgin subfamily A member 4 is a protein that in humans is encoded by the GOLGA4 gene.

ADP-ribosylation factor 5 is a protein that in humans is encoded by the ARF5 gene.

AP-1 complex subunit gamma-like 2 is a protein that in humans is encoded by the AP1G2 gene.

ADP-ribosylation factor-like protein 1 is a protein that in humans is encoded by the ARL1 gene.

Synergin gamma also known as AP1 subunit gamma-binding protein 1 (AP1GBP1) is a protein that in humans is encoded by the SYNRG gene.

Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 is a protein that in humans is encoded by the ASAP2 gene.

ADP-ribosylation factor-related protein 1 is a protein that in humans is encoded by the ARFRP1 gene.

Low density lipoprotein receptor-related protein 3 (LRP-3) is a protein that in humans is encoded by the LRP3 gene.

Clathrin adaptor proteins, also known as adaptins, are vesicular transport adaptor proteins associated with clathrin. These proteins are synthesized in the ribosomes, processed in the endoplasmic reticulum and transported from the Golgi apparatus to the trans-Golgi network, and from there via small carrier vesicles to their final destination compartment. The association between adaptins and clathrin are important for vesicular cargo selection and transporting. Clathrin coats contain both clathrin and adaptor complexes that link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Therefore, adaptor proteins are responsible for the recruitment of cargo molecules into a growing clathrin-coated pits. The two major types of clathrin adaptor complexes are the heterotetrameric vesicular transport adaptor proteins (AP1-5), and the monomeric GGA adaptors. Adaptins are distantly related to the other main type of vesicular transport proteins, the coatomer subunits, sharing between 16% and 26% of their amino acid sequence.

The C-terminal domain ofBeta2-adaptin is a protein domain is involved in cell trafficking by aiding import and export of substances in and out of the cell.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000100083 - Ensembl, May 2017
1 2 3 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 . hdl: 2445/176753 . 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. S2CID 21977507.
↑ 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.

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. S2CID 10348751.
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. S2CID 30836125.
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. S2CID 21977507.
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. S2CID 4395774.
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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000100083 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid10747088-5] 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.

[pmid10747089-6] 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.

[pmid16407204-7] 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 . hdl: 2445/176753 . PMID 16407204.

[entrez-8] "Entrez Gene: GGA1 golgi associated, gamma adaptin ear containing, ARF binding protein 1".

[pmid11821067-9] 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.

[pmid12135764-10] 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.

[pmid12505986-11] 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.

[pmid12221117-12] 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.

[pmid10749927-13] 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.

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GGA1

Contents

Interactions

Related Research Articles

References

Further reading