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Vol. 12, Issue 4, 1035-1045, April 2001
and
*Friedrich Miescher Laboratorium, Max Planck
Gesellschaft, D-72076 Tübingen, Germany; and The activation of the small ras-like GTPase Arf1p requires the
action of guanine nucleotide exchange factors. Four Arf1p guanine nucleotide exchange factors have been identified in yeast: Sec7p, Syt1p, Gea1p, and its homologue Gea2p. We identified
GEA2 as a multicopy suppressor of a
sec21-3 temperature-sensitive mutant. SEC21 encodes the Department of
Molecular and Cell Biology and Howard Hughes Medical Institute,
University of California, Berkeley, California 94720
-subunit of coatomer, a heptameric
protein complex that together with Arf1p forms the COPI coat.
GEA1 and GEA2 have at least partially
overlapping functions, because deletion of either gene results in no
obvious phenotype, whereas the double null mutant is inviable.
Conditional mutants defective in both GEA1 and
GEA2 accumulate endoplasmic reticulum and Golgi
membranes under restrictive conditions. The two genes do not serve
completely overlapping functions because a 
gea1
arf1 mutant is not more sickly than a
arf1 strain, whereas gea2
arf1 is inviable. Biochemical experiments revealed
similar distributions and activities for the two proteins. Gea1p and
Gea2p exist both in membrane-bound and in soluble forms. The
membrane-bound forms, at least one of which, Gea2p, can be visualized
on Golgi structures, are both required for vesicle budding and protein
transport from the Golgi to the endoplasmic reticulum. In contrast,
Sec7p, which is required for protein transport within the Golgi, is not
required for retrograde protein trafficking.
Corresponding author. E-mail:
anne.spang{at}tuebingen.mpg.de.
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