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Vol. 12, Issue 6, 1885-1896, June 2001
and
*Department of Biological Chemistry, University of California
Los Angeles School of Medicine, Los Angeles, California 90095-1737; and
Gga proteins represent a newly recognized, evolutionarily conserved
protein family with homology to the "ear" domain of the clathrin
adaptor AP-1 Division of Cellular and Molecular Medicine and Howard
Hughes Medical Institute, University of California San Diego School of
Medicine, La Jolla, CA 92093-0668
subunit. Yeast cells contain two Gga proteins, Gga1p
and Gga2p, that have been proposed to act in transport between the
trans-Golgi network and endosomes. Here we
provide genetic and physical evidence that yeast Gga proteins function
in trans-Golgi network clathrin coats. Deletion of Gga2p
(gga2
), the major Gga protein, accentuates growth and
-factor maturation defects in cells carrying a temperature-sensitive
allele of the clathrin heavy chain gene. Cells carrying either
gga2 or a deletion of the AP-1 
subunit gene
(apl2) alone are phenotypically
normal, but cells carrying both gga2 and
apl2 are defective in growth, -factor maturation,
and transport of carboxypeptidase S to the vacuole. Disruption of both
GGA genes and APL2 results in cells so
severely compromised in growth that they form only microcolonies. Gga
proteins can bind clathrin in vitro and cofractionate with clathrin-coated vesicles. Our results indicate that yeast Gga proteins
play an important role in cargo-selective clathrin-mediated protein
traffic from the trans-Golgi network to endosomes.
These authors contributed equally.
§
Present address: Department of Genetics, Cell
Biology and Development, University of Minnesota, Twin Cities, St.
Paul, MN 55108.
Corresponding author. E-mail address:
gpayne{at}mednet.ucla.edu.
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