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(Received for publication, August 7, 1996, and in revised form, December 19, 1996)
From the Howard Hughes Medical Institute and the Department of
Molecular Physiology and Biophysics and Pharmacology, Vanderbilt
University School of Medicine, Nashville, Tennessee 37232
ADP-ribosylation factors (ARFs) have been
implicated in vesicle transport in the Golgi complex. 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. The mRNA of arfaptin 1 was ubiquitously expressed, and recombinant arfaptin 1 bound
preferentially to class I ARFs, especially ARF1, but only in the
GTP-bound form. The interactions were independent of myristoylation of
ARF. Arfaptin 1 in cytosol was recruited to Golgi membranes by ARF in a
guanosine 5
-O-(3-thiotriphosphate)-dependent
and brefeldin A-sensitive manner. When expressed in COS cells, arfaptin
1 was localized to the Golgi complex. The yeast two-hybrid system
yielded another clone, which encoded a putative protein, which we have
named arfaptin 2. This consisted of the same number of amino acids as
arfaptin 1 and was 60% identical to it. Arfaptin 2 was also
ubiquitously expressed and bound to the GTP-, but not GDP-liganded form
of class I ARFs, especially ARF1. These results suggest that arfaptins 1 and 2 may be direct target proteins of class 1 ARFs. Arfaptin 1 may
be involved in Golgi function along with ARF1.
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