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ARFIP1  -  ADP-ribosylation factor interacting protein 1

Homo sapiens

Synonyms: ADP-ribosylation factor-interacting protein 1, Arfaptin-1, HSU52521
 
 
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High impact information on ARFIP1

 

Biological context of ARFIP1

  • Employing yeast two-hybrid screening of an HL60 cDNA library using a constitutively active mutant of ARF3 (ARF3.Q71L), as a probe, we have identified a cDNA encoding a novel protein with a calculated molecular mass of 38.6 kDa, which we have named arfaptin 1 [4].
  • Utilizing several deletion mutants of arfaptin 1 it is shown that the association of arfaptin 1 with myrARF3 is mediated via two binding sites on arfaptin 1 [5].
 

Anatomical context of ARFIP1

 

Associations of ARFIP1 with chemical compounds

  • Arfaptin effects on guanine nucleotide binding by ARFs were minimal whether or not a purified ARF guanine nucleotide-exchange protein was present [3].
 

Other interactions of ARFIP1

  • Arfaptin 1 inhibited activation of both enzymes in a concentration-dependent manner and was without effect in the absence of ARF [3].
  • However, a second group reported that POR1, a truncated form of arfaptin, bound to GTP-Rac1 [6].
  • Here it is shown that the dimeric helical domain of Arfaptin superimposes with a monomeric helical domain from the Dbl homology domain of Tiam, a guanine nucleotide exchange factor (GEF) for Rac, in their respective complexes with Rac [7].
  • PICK1 is a 416 amino acid protein that contains a PDZ domain, a coiled-coil motif/arfaptin homology domain and an acidic c-terminal [8].
  • This view has been challenged by recent structural and biochemical studies of the Arfaptin/Por protein, which interacts equally well with the GDP- and GTP-bound forms of the G protein Rac [7].

References

  1. The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. Tarricone, C., Xiao, B., Justin, N., Walker, P.A., Rittinger, K., Gamblin, S.J., Smerdon, S.J. Nature (2001) [Pubmed]
  2. Phosphorylation of arfaptin 2 at Ser260 by Akt Inhibits PolyQ-huntingtin-induced toxicity by rescuing proteasome impairment. Rangone, H., Pardo, R., Colin, E., Girault, J.A., Saudou, F., Humbert, S. J. Biol. Chem. (2005) [Pubmed]
  3. Effects of arfaptin 1 on guanine nucleotide-dependent activation of phospholipase D and cholera toxin by ADP-ribosylation factor. Tsai, S.C., Adamik, R., Hong, J.X., Moss, J., Vaughan, M., Kanoh, H., Exton, J.H. J. Biol. Chem. (1998) [Pubmed]
  4. Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes. Kanoh, H., Williger, B.T., Exton, J.H. J. Biol. Chem. (1997) [Pubmed]
  5. Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits phospholipase D. Williger, B.T., Provost, J.J., Ho, W.T., Milstine, J., Exton, J.H. FEBS Lett. (1999) [Pubmed]
  6. Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1. Shin, O.H., Exton, J.H. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  7. Structural mimicry of DH domains by Arfaptin suggests a model for the recognition of Rac-GDP by its guanine nucleotide exchange factors. Cherfils, J. FEBS Lett. (2001) [Pubmed]
  8. PDZ domain protein-protein interactions: a case study with PICK1. Dev, K.K. Current topics in medicinal chemistry (2007) [Pubmed]
 
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