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Vol. 12, Issue 4, 957-969, April 2001
Department of Biochemistry, Dartmouth Medical School, Hanover, New
Hampshire 03755
Yeast cells lacking a functional p24 complex accumulate a subset of
secretory proteins in the endoplasmic reticulum (ER) and increase the
extracellular secretion of HDEL-containing ER residents such as
Kar2p/BiP. We report that a loss of p24 function causes activation of
the unfolded protein response (UPR) and leads to increased
KAR2 expression. The HDEL receptor (Erd2p) is functional and traffics in p24 deletion strains as in wild-type strains, however
the capacity of the retrieval pathway is exceeded. Other conditions
that activate the UPR and elevate KAR2 expression also lead to extracellular secretion of Kar2p. Using an in vitro assay that
reconstitutes budding from the ER, we detect elevated levels of Kar2p
in ER-derived vesicles from p24 deletion strains and from
wild-type strains with an activated UPR. Silencing the UPR by
IRE1 deletion diminished Kar2p secretion under these
conditions. We suggest that activation of the UPR plays a major role in
extracellular secretion of Kar2p.
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