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Vol. 11, Issue 10, 3469-3484, October 2000
and
*Department of Molecular Cell Research, Max-Planck-Institute for
Medical Research, D-69120 Heidelberg, Germany; and
Localization of soluble endoplasmic reticulum (ER) resident
proteins is likely achieved by the complementary action of retrieval and retention mechanisms. Whereas the machinery involving the H/KDEL
and related retrieval signals in targeting escapees back to the ER is
well characterized, other mechanisms including retention are still
poorly understood. We have identified a protein disulfide isomerase
(Dd-PDI) lacking the HDEL retrieval signal normally found at the C
terminus of ER residents in Dictyostelium discoideum. Here we demonstrate that its 57 residue C-terminal domain is necessary for intracellular retention of Dd-PDI and sufficient to localize a
green fluorescent protein (GFP) chimera to the ER, especially to the
nuclear envelope. Dd-PDI and GFP-PDI57 are recovered in similar
cation-dependent complexes. The overexpression of GFP-PDI57 leads to
disruption of endogenous PDI complexes and induces the secretion of
PDI, whereas overexpression of a GFP-HDEL chimera induces the secretion
of endogenous calreticulin, revealing the presence of two independent
and saturable mechanisms. Finally, low-level expression of Dd-PDI but
not of PDI truncated of its 57 C-terminal residues complements the
otherwise lethal yeast TRG1/PDI1 null mutation, demonstrating
functional disulfide isomerase activity and ER localization.
Altogether, these results indicate that the PDI57 peptide contains ER
localization determinants recognized by a conserved machinery present
in D. discoideum and Saccharomyces cerevisiae.
Department of Neurobiology, Max-Planck-Institute for
Biophysical Chemistry, D-37077, Göttingen, Germany
Corresponding author. E-mail address:
soldati{at}mpimf-heidelberg.mpg.de.
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