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A more recent version of this article appeared on August 1, 2002
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Submitted on April 5, 2002
Revised on May 12, 2002
Accepted on May 17, 2002
1 Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Blvd., Dallas, TX 75235-9038
* Corresponding author. E-mail address: michael.roth{at}utsouthwestern.edu.
ARF GAP1, a 415 amino acid GTPase activating protein (GAP) for ADP-ribosylation factor (ARF) contains an amino-terminal 115 amino acid catalytic domain and no other recognizable features. Amino acids 203 to 334 of ARF GAP1 were sufficient to target a GFP-fusion protein to Golgi membranes in vivo. When over-expressed in COS-1 cells, this protein domain inhibited protein transport between the ER and Golgi and, in vitro, competed with the full-length ARF GAP1 for binding to membranes. Membrane-binding by ARF GAP1 in vitro was increased by a factor in cytosol and this increase was inhibited by IC261, an inhibitor selective for casein kinase I
(CKI), or when cytosol was treated with antibody to CKI. The non-catalytic domain of ARF GAP1 was phosphorylated both in vivo and in vitro by CKI. IC261 blocked membrane binding by ARF GAP1 in vivo and inhibited protein transport in the early secretory pathway. Over-expression of a catalytically inactive CKI also inhibited the binding of ARF GAP1 to membranes and interfered with protein transport. Thus, a CKI isoform is required for protein traffic through the early secretory pathway and can modulate the amount of ARF GAP1 that can bind to membranes.
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