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ARD1/TRIM23

  • Reference work entry
  • First Online:
Encyclopedia of Signaling Molecules

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Synonyms

ADP-ribosylation factor; Arf-domain protein; Domain protein; Tripartite motif protein 23

Historical Background

ARD1 was first described in 1993 as the deduced protein product of clones isolated from human and rat genomic cDNA libraries that encoded an about 18-kDa ADP-ribosylation factor (Arf) sequence at the C-terminus of a 64-kDa molecule (Mishima et al. 1993). Human ARD1 coding region cDNA hybridized with 3.7- and 4.1-kb mRNAs from all rat tissues examined. Both recombinant, full-length ARD1 and its Arf domain (M403-A574), activated cholera toxin ADP-ribosyltransferase activity, at that time a defining characteristic of Arf function, whereas the non-Arf (M1-K402) fragment of ARD1 did not. Using recombinant proteins on nitrocellulose membranes, only the Arf domain (and a recombinant ARF3), not the full-length ARD1, bound radio-labeled GTP (Mishima et al. 1993).

Further investigation of GTPase activity of the same recombinant proteins in solution provided evidence that the...

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References

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  • Meza-Carmen V, Pacheco-Rodriguez G, Soo Kang G, Kato J, Donati C, Zhang C, Vichi A, Payne DM, El-Chemaly S, Stylianou M, Moss J, Vaughan M. Regulation of growth factor receptor degradation by ADP-ribosylation factor domain protein (ARD)1. Proc Natl Acad Sci U S A. 2011;108:10454–9.

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  • Vitale N, Moss J, Vaughan M. Interaction of the GTP-binding and GTPase-activating domains of ARD1 involves the effector region of the ADP-ribosylation factor domain. J Biol Chem. 1997a;272:3897–904.

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  • Vitale N, Moss J, Vaughan M. Characterization of a GDP dissociation inhibitory region of ADP-ribosylation factor domain protein ARD1. J Biol Chem. 1997b;272:25077–82.

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  • Vitale N, Moss J, Vaughan M. Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1). J Biol Chem. 1998a;273:2553–60.

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  • Vitale N, Horiba K, Ferrans V, Moss J, Vaughan M. Localization of ADP-ribosylation factor domain protein 1 (ARD1) in lysosomes and Golgi apparatus. Proc Natl Acad Sci U S A. 1998b;95:8613–8.

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  • Vitale N, Ferrans V, Moss J, Vaughan M. Identification of lysosomal and Golgi localization signals in GAP and ARF domains of ARF domain protein 1. Mol Cell Biol. 2000a;20:7432–52.

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  • Vitale N, Pacheco-Rodriguez G, Ferrans V, Riemenschneider W, Moss J, Vaughan M. Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1). J Biol Chem. 2000b;275:21331–9.

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Author information

Authors and Affiliations

  1. Cardiovascular and Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA

    Joel Moss & Martha Vaughan

Authors
  1. Joel Moss
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  2. Martha Vaughan
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Corresponding author

Correspondence to Joel Moss .

Editor information

Editors and Affiliations

  1. Department of Molecular Science and Technology, Ajou University, Suwon, Korea

    Sangdun Choi

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Moss, J., Vaughan, M. (2018). ARD1/TRIM23. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_644

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