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Vol. 10, Issue 8, 2573-2582, August 1999
and
*School of Biological Sciences, University of Manchester,
Manchester, M13 9PT, United Kingdom; ERp57 is a lumenal protein of the endoplasmic reticulum (ER) and a
member of the protein disulfide isomerase (PDI) family. In contrast to
archetypal PDI, ERp57 interacts specifically with newly synthesized
glycoproteins. In this study we demonstrate that ERp57 forms discrete
complexes with the ER lectins, calnexin and calreticulin. Specific
ERp57/calreticulin complexes exist in canine pancreatic microsomes, as
demonstrated by SDS-PAGE after cross-linking, and by native
electrophoresis in the absence of cross-linking. After in vitro
translation and import into microsomes, radiolabeled ERp57 can be
cross-linked to endogenous calreticulin and calnexin while radiolabeled
PDI cannot. Likewise, radiolabeled calreticulin is cross-linked to
endogenous ERp57 but not PDI. Similar results were obtained in Lec23
cells, which lack the glucosidase I necessary to produce glycoprotein
substrates capable of binding to calnexin and calreticulin. This
observation indicates that ERp57 interacts with both of the ER lectins
in the absence of their glycoprotein substrate. This result was
confirmed by a specific interaction between in vitro synthesized
calreticulin and ERp57 prepared in solution in the absence of other ER
components. We conclude that ERp57 forms complexes with both calnexin
and calreticulin and propose that it is these complexes that can
specifically modulate glycoprotein folding within the ER lumen.
Department of
Physiology, University of Texas Health Science Center, San Antonio,
Texas 78284; and Department of Medical
Biochemistry, University of Wales College of Medicine, Heath Park,
Cardiff, CF4 4XN, United Kingdom
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