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ARF3  -  ADP-ribosylation factor 3

Bos taurus

 
 
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High impact information on ARF3

  • Partial purification yielded an approximately 60-kDa BFA-insensitive GEP that enhanced binding of ARF1 and ARF3 to Golgi membranes [1].
  • Release of bound [35S]GTP gamma S from ARF3 required the presence of both GEP and unlabeled GTP or GTP gamma S; GDP was much less effective [1].
  • The fact that the sizes of these mRNAs are similar to those of other ARFs (ARF 1, 1.9 kb; ARF 2, 2.6 kb; ARF 3, approximately 3.8 and 1.3 kb; ARF 4, 1.8 kb) explain the previously observed inconsistencies between the cDNA and ARF-specific oligonucleotide hybridization patterns [2].

References

  1. Purification and characterization of a guanine nucleotide-exchange protein for ADP-ribosylation factor from spleen cytosol. Tsai, S.C., Adamik, R., Moss, J., Vaughan, M. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  2. Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells. Tsuchiya, M., Price, S.R., Tsai, S.C., Moss, J., Vaughan, M. J. Biol. Chem. (1991) [Pubmed]
 
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