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ADP-ribosylation factor-like protein 1 is a protein that in humans is encoded by the ARL1gene.[5]
Function
The protein encoded by this gene belongs to the ARL (ADP-ribosylation factor-like) family of proteins, which are structurally related to ADP-ribosylation factors (ARFs). ARFs, described as activators of cholera toxin (CT) ADP-ribosyltransferase activity, regulate intracellular vesicular membrane trafficking, and stimulate a phospholipase D (PLD) isoform. Although, ARL proteins were initially thought not to activate CT or PLD, later work showed that they are weak stimulators of PLD and CT in a phospholipid dependent manner.[5]
^Van Valkenburgh H, Shern JF, Sharer JD, Zhu X, Kahn RA (June 2001). "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins". J. Biol. Chem. 276 (25): 22826–37. doi:10.1074/jbc.M102359200. PMID11303027.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Further reading
Zhang GF, Patton WA, Lee FJ, Liyanage M, Han JS, Rhee SG, Moss J, Vaughan M (1995). "Different ARF domains are required for the activation of cholera toxin and phospholipase D". J. Biol. Chem. 270 (1): 21–4. doi:10.1074/jbc.270.1.21. PMID7814376.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Hong JX, Lee FJ, Patton WA, Lin CY, Moss J, Vaughan M (1998). "Phospholipid- and GTP-dependent activation of cholera toxin and phospholipase D by human ADP-ribosylation factor-like protein 1 (HARL1)". J. Biol. Chem. 273 (25): 15872–6. doi:10.1074/jbc.273.25.15872. PMID9624189.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Zhao L, Helms JB, Brunner J, Wieland FT (1999). "GTP-dependent binding of ADP-ribosylation factor to coatomer in close proximity to the binding site for dilysine retrieval motifs and p23". J. Biol. Chem. 274 (20): 14198–203. doi:10.1074/jbc.274.20.14198. PMID10318838.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Van Valkenburgh H, Shern JF, Sharer JD, Zhu X, Kahn RA (2001). "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins". J. Biol. Chem. 276 (25): 22826–37. doi:10.1074/jbc.M102359200. PMID11303027.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415-8. doi:10.1093/nar/gkj139. PMC1347501. PMID16381901.
Zahn C, Hommel A, Lu L, Hong W, Walther DJ, Florian S, Joost HG, Schürmann A (2007). "Knockout of Arfrp1 leads to disruption of ARF-like1 (ARL1) targeting to the trans-Golgi in mouse embryos and HeLa cells". Mol. Membr. Biol. 23 (6): 475–85. doi:10.1080/09687860600840100. PMID17127620.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC1847948. PMID17353931.