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Vol. 12, Issue 12, 3783-3796, December 2001
and
Department of Molecular Biology, Princeton University, Princeton,
New Jersey 08544
DSL1 was identified through its genetic interaction
with SLY1, which encodes a t-SNARE-interacting protein
that functions in endoplasmic reticulum (ER)-to-Golgi traffic.
Conditional dsl1 mutants exhibit a block in ER-to-Golgi
traffic at the restrictive temperature. Here, we show that
dsl1 mutants are defective for retrograde Golgi-to-ER
traffic, even under conditions where no anterograde transport block is
evident. These results suggest that the primary function of Dsl1p may
be in retrograde traffic, and that retrograde defects can lead to
secondary defects in anterograde traffic. Dsl1p is an ER-localized
peripheral membrane protein that can be extracted from the membrane in
a multiprotein complex. Immunoisolation of the complex yielded Dsl1p
and proteins of ~80 and ~55 kDa. The ~80-kDa protein has been
identified as Tip20p, a protein that others have shown to exist in a
tight complex with Sec20p, which is ~50 kDa. Both Sec20p and Tip20p
function in retrograde Golgi-to-ER traffic, are ER-localized, and bind
to the ER t-SNARE Ufe1p. These findings suggest that an ER-localized
complex of Dsl1p, Sec20p, and Tip20p functions in retrograde traffic,
perhaps upstream of a Sly1p/Ufe1p complex. Last, we show that Dsl1p
interacts with the 
-subunit of the retrograde COPI coat, Ret2p, and
discuss possible roles for this interaction.
Present address: Department of Molecular Biology
and Microbiology, Tufts University School of Medicine, Boston, MA 02111.
Corresponding author. E-mail address:
gwaters{at}molbio.princeton.edu.
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