ARF1

El factor 1 de ribosilación de ADP es una proteína que en los humanos está codificada por el gen ARF1. ^[1]

Función editar

El factor de ribosilación de ADP 1 (ARF1) es un miembro de la familia de genes ARF humanos. Los miembros de la familia codifican pequeñas proteínas de unión a nucleótidos de guanina que estimulan la actividad ADP-ribosiltransferasa de la toxina del cólera y desempeñan un papel en el tráfico vesicular como activadores de la fosfolipasa D. Los productos genéticos, incluidas 6 proteínas ARF y 11 proteínas similares a ARF, constituyen una familia de la superfamilia RAS. Las proteínas ARF se clasifican en clase I (ARF1, ARF2 y ARF3), clase II (ARF4 y ARF5) y clase III (ARF6), y los miembros de cada clase comparten una organización genética común. La proteína ARF1 está localizada en el aparato de Golgi y tiene un papel central en el transporte intra-Golgi. Para este gen se han encontrado múltiples variantes de transcripción empalmadas alternativamente que codifican la misma proteína. ^[2]

El principal mecanismo de acción de Brefeldin A es mediante la inhibición de ARF1.

Interacciones editar

Se ha demostrado que ARF1 interactúa con:

CHRM3, ^[3]
COPB1, ^[4] ^[5]
GGA3, ^[6] ^[7] y
PLD2. ^[8] ^[9]

Referencias editar

↑ Lee CM, Haun RS, Tsai SC, Moss J, Vaughan M (June 1992). «Characterization of the human gene encoding ADP-ribosylation factor 1, a guanine nucleotide-binding activator of cholera toxin». J Biol Chem 267 (13): 9028-34. PMID 1577740. doi:10.1016/S0021-9258(19)50383-0.
↑ «Entrez Gene: ARF1 ADP-ribosylation factor 1».
↑ Mitchell R, Robertson DN, Holland PJ, Collins D, Lutz EM, Johnson MS (September 2003). «ADP-ribosylation factor-dependent phospholipase D activation by the M3 muscarinic receptor». J. Biol. Chem. 278 (36): 33818-30. PMID 12799371. doi:10.1074/jbc.M305825200.
↑ Fischer KD, Helms JB, Zhao L, Wieland FT (April 2000). «Site-specific photocrosslinking to probe interactions of Arf1 with proteins involved in budding of COPI vesicles». Methods 20 (4): 455-64. PMID 10720466. doi:10.1006/meth.2000.0958.
↑ Eugster A, Frigerio G, Dale M, Duden R (August 2000). «COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP». EMBO J. 19 (15): 3905-17. PMC 306616. PMID 10921873. doi:10.1093/emboj/19.15.3905.
↑ 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». J. Cell Biol. 149 (1): 81-94. PMC 2175099. PMID 10747089. doi:10.1083/jcb.149.1.81.
↑ 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. PMID 11301005. doi:10.1016/s0092-8674(01)00299-9.
↑ Lee S, Park JB, Kim JH, Kim Y, Kim JH, Shin KJ, Lee JS, Ha SH, Suh PG, Ryu SH (July 2001). «Actin directly interacts with phospholipase D, inhibiting its activity». J. Biol. Chem. 276 (30): 28252-60. PMID 11373276. doi:10.1074/jbc.M008521200.
↑ Park JB, Kim JH, Kim Y, Ha SH, Yoo JS, Du G, Frohman MA, Suh PG, Ryu SH (July 2000). «Cardiac phospholipase D2 localizes to sarcolemmal membranes and is inhibited by alpha-actinin in an ADP-ribosylation factor-reversible manner». J. Biol. Chem. 275 (28): 21295-301. PMID 10801846. doi:10.1074/jbc.M002463200.

Otras lecturas editar

Serafini T, Orci L, Amherdt M (1991). «ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein.». Cell 67 (2): 239-53. PMID 1680566. S2CID 9766090. doi:10.1016/0092-8674(91)90176-Y.
Kahn RA, Kern FG, Clark J (1991). «Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins.». J. Biol. Chem. 266 (4): 2606-14. PMID 1899243. doi:10.1016/S0021-9258(18)52288-2.
Stearns T, Willingham MC, Botstein D, Kahn RA (1990). «ADP-ribosylation factor is functionally and physically associated with the Golgi complex.». Proc. Natl. Acad. Sci. U.S.A. 87 (3): 1238-42. Bibcode:1990PNAS...87.1238S. PMC 53446. PMID 2105501. doi:10.1073/pnas.87.3.1238.
Bobak DA, Nightingale MS, Murtagh JJ (1989). «Molecular cloning, characterization, and expression of human ADP-ribosylation factors: two guanine nucleotide-dependent activators of cholera toxin.». Proc. Natl. Acad. Sci. U.S.A. 86 (16): 6101-5. Bibcode:1989PNAS...86.6101B. PMC 297783. PMID 2474826. doi:10.1073/pnas.86.16.6101.
Greasley SE, Jhoti H, Teahan C (1995). «The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms.». Nat. Struct. Biol. 2 (9): 797-806. PMID 7552752. S2CID 9461256. doi:10.1038/nsb0995-797.
Welsh CF, Moss J, Vaughan M (1995). «ADP-ribosylation factors: a family of approximately 20-kDa guanine nucleotide-binding proteins that activate cholera toxin.». Mol. Cell. Biochem. 138 (1–2): 157-66. PMID 7898460. S2CID 42819002. doi:10.1007/BF00928458.
Greasley S, Jhoti H, Fensome AC (1995). «Crystallization and preliminary X-ray diffraction studies on ADP-ribosylation factor 1». J. Mol. Biol. 244 (5): 651-3. PMID 7990146. doi:10.1006/jmbi.1994.1759.
Amor JC, Harrison DH, Kahn RA, Ringe D (1994). «Structure of the human ADP-ribosylation factor 1 complexed with GDP». Nature 372 (6507): 704-8. Bibcode:1994Natur.372..704C. PMID 7990966. S2CID 4362056. doi:10.1038/372704a0.
Dascher C, Balch WE (1994). «Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus». J. Biol. Chem. 269 (2): 1437-48. PMID 8288610. doi:10.1016/S0021-9258(17)42277-0.
Rümenapp U, Geiszt M, Wahn F (1996). «Evidence for ADP-ribosylation-factor-mediated activation of phospholipase D by m3 muscarinic acetylcholine receptor». Eur. J. Biochem. 234 (1): 240-4. PMID 8529647. doi:10.1111/j.1432-1033.1995.240_c.x.
Andersson B, Wentland MA, Ricafrente JY (1996). «A "double adaptor" method for improved shotgun library construction». Anal. Biochem. 236 (1): 107-13. PMID 8619474. doi:10.1006/abio.1996.0138.
Hirai M, Kusuda J, Hashimoto K (1997). «Assignment of human ADP ribosylation factor (ARF) genes ARF1 and ARF3 to chromosomes 1q42 and 12q13, respectively». Genomics 34 (2): 263-5. PMID 8661066. doi:10.1006/geno.1996.0283.
Kanoh H, Williger BT, Exton JH (1997). «Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes». J. Biol. Chem. 272 (9): 5421-9. PMID 9038142. doi:10.1074/jbc.272.9.5421.
Yu W, Andersson B, Worley KC (1997). «Large-scale concatenation cDNA sequencing». Genome Res. 7 (4): 353-8. PMC 139146. PMID 9110174. doi:10.1101/gr.7.4.353.
Shome K, Vasudevan C, Romero G (1997). «ARF proteins mediate insulin-dependent activation of phospholipase D». Curr. Biol. 7 (6): 387-96. Bibcode:1997CBio....7..387S. PMID 9197239. S2CID 9609409. doi:10.1016/S0960-9822(06)00186-2.
Frank S, Upender S, Hansen SH, Casanova JE (1998). «ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6». J. Biol. Chem. 273 (1): 23-7. PMID 9417041. doi:10.1074/jbc.273.1.23.
Betz SF, Schnuchel A, Wang H (1998). «Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1». Proc. Natl. Acad. Sci. U.S.A. 95 (14): 7909-14. Bibcode:1998PNAS...95.7909B. PMC 20903. PMID 9653114. doi:10.1073/pnas.95.14.7909.
Kim JH, Lee SD, Han JM (1998). «Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA». FEBS Lett. 430 (3): 231-5. PMID 9688545. S2CID 36075513. doi:10.1016/S0014-5793(98)00661-9.
Huber I, Cukierman E, Rotman M (1998). «Requirement for both the amino-terminal catalytic domain and a noncatalytic domain for in vivo activity of ADP-ribosylation factor GTPase-activating protein». J. Biol. Chem. 273 (38): 24786-91. PMID 9733781. doi:10.1074/jbc.273.38.24786.

Datos: Q17831452

[pmid1577740-1] Lee CM, Haun RS, Tsai SC, Moss J, Vaughan M (June 1992). «Characterization of the human gene encoding ADP-ribosylation factor 1, a guanine nucleotide-binding activator of cholera toxin». J Biol Chem 267 (13): 9028-34. PMID 1577740. doi:10.1016/S0021-9258(19)50383-0.

[2] «Entrez Gene: ARF1 ADP-ribosylation factor 1».

[pmid12799371-3] Mitchell R, Robertson DN, Holland PJ, Collins D, Lutz EM, Johnson MS (September 2003). «ADP-ribosylation factor-dependent phospholipase D activation by the M3 muscarinic receptor». J. Biol. Chem. 278 (36): 33818-30. PMID 12799371. doi:10.1074/jbc.M305825200.

[pmid10720466-4] Fischer KD, Helms JB, Zhao L, Wieland FT (April 2000). «Site-specific photocrosslinking to probe interactions of Arf1 with proteins involved in budding of COPI vesicles». Methods 20 (4): 455-64. PMID 10720466. doi:10.1006/meth.2000.0958.

[pmid10921873-5] Eugster A, Frigerio G, Dale M, Duden R (August 2000). «COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP». EMBO J. 19 (15): 3905-17. PMC 306616. PMID 10921873. doi:10.1093/emboj/19.15.3905.

[pmid10747089-6] 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». J. Cell Biol. 149 (1): 81-94. PMC 2175099. PMID 10747089. doi:10.1083/jcb.149.1.81.

[pmid11301005-7] 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. PMID 11301005. doi:10.1016/s0092-8674(01)00299-9.

[pmid11373276-8] Lee S, Park JB, Kim JH, Kim Y, Kim JH, Shin KJ, Lee JS, Ha SH, Suh PG, Ryu SH (July 2001). «Actin directly interacts with phospholipase D, inhibiting its activity». J. Biol. Chem. 276 (30): 28252-60. PMID 11373276. doi:10.1074/jbc.M008521200.

[pmid10801846-9] Park JB, Kim JH, Kim Y, Ha SH, Yoo JS, Du G, Frohman MA, Suh PG, Ryu SH (July 2000). «Cardiac phospholipase D2 localizes to sarcolemmal membranes and is inhibited by alpha-actinin in an ADP-ribosylation factor-reversible manner». J. Biol. Chem. 275 (28): 21295-301. PMID 10801846. doi:10.1074/jbc.M002463200.

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