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J Biol Chem, Vol. 274, Issue 51, 36609-36615, December 17, 1999
From the Howard Hughes Medical Institute and Department of
Molecular Physiology and Biophysics, Vanderbilt University School of
Medicine, Nashville, Tennessee 37232
Yeast two-hybrid screening of a human kidney
cDNA library using the GTP-bound form of a class II
ADP-ribosylation factor (ARF5) identified a novel ARF5-binding protein
with a calculated molecular mass of 82.4 kDa, which was named
arfophilin. Northern hybridization analysis showed high level
arfophilin mRNA expression in human heart and skeletal muscle.
Arfophilin bound only to the active, GTP-bound form of ARF5 and did not
bind to GTP-ARF3, which is a class I ARF. The N terminus of ARF5 (1-17
amino acids) was essential for binding to arfophilin. The GTP-bound
form of ARF5 with amino acid residues in the N terminus mutated to
those in ARF4 (another class II ARF) also bound to arfophilin,
suggesting it is a target protein for GTP-bound forms of class II ARFs.
The binding site for ARF on arfophilin was localized to the C terminus
(residues 612-756), which contains putative coiled-coil structures.
Recombinant arfophilin overexpressed in CHO-K1 cells was localized in
the cytosol and translocated to a membrane fraction in association with
GTP-bound ARF5. ARF5 containing the N terminus of ARF3 did not promote
translocation indicating that class II ARFs are specific carriers for arfophilin.
Identification of Arfophilin, a Target Protein for GTP-bound
Class II ADP-ribosylation Factors*
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Investigator of the Howard Hughes Medical Institute. To whom all
correspondence should be addressed. Tel.: 615-322-6494; Fax: 615-322-4381; E-mail: john.exton@mcmail.vanderbilt.edu.
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