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Vol. 10, Issue 3, 537-549, March 1999
Division of Hematology, Department of Internal Medicine, Washington
University School of Medicine, St. Louis, Missouri 63110
The GTP-binding protein ADP-ribosylation factor (ARF) initiates
clathrin-coat assembly at the trans-Goli network (TGN) by generating
high-affinity membrane-binding sites for the AP-1 adaptor complex. Both
transmembrane proteins, which are sorted into the assembling coated
bud, and novel docking proteins have been suggested to be partners with
GTP-bound ARF in generating the AP-1-docking sites. The best
characterized, and probably the major transmembrane molecules sorted
into the clathrin-coated vesicles that form on the TGN, are the mannose
6-phosphate receptors (MPRs). Here, we have examined the role of the
MPRs in the AP-1 recruitment process by comparing fibroblasts derived
from embryos of either normal or MPR-negative animals. Despite major
alterations to the lysosome compartment in the MPR-deficient cells, the
steady-state distribution of AP-1 at the TGN is comparable to that of
normal cells. Golgi-enriched membranes prepared from the
receptor-negative cells also display an apparently normal capacity to
recruit AP-1 in vitro in the presence of ARF and either GTP or GTP
S.
The AP-1 adaptor is recruited specifically onto the TGN and not onto
the numerous abnormal membrane elements that accumulate within the
MPR-negative fibroblasts. AP-1 bound to TGN membranes from either
normal or MPR-negative fibroblasts is fully resistant to chemical
extraction with 1 M Tris-HCl, pH 7, indicating that the adaptor binds
to both membrane types with high affinity. The only difference we do
note between the Golgi prepared from the MPR-deficient cells and the
normal cells is that AP-1 recruited onto the receptor-lacking membranes in the presence of ARF1·GTP is consistently more resistant to extraction with Tris. Because sensitivity to Tris extraction correlates well with nucleotide hydrolysis, this finding might suggest a possible
link between MPR sorting and ARF GAP regulation. We conclude that the
MPRs are not essential determinants in the initial steps of AP-1
binding to the TGN but, instead, they may play a regulatory role in
clathrin-coated vesicle formation by affecting ARF·GTP hydrolysis.
Corresponding author. e-mail: skornfel{at}im.wustl.edu.
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