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Vol. 13, Issue 12, 4456-4469, December 2002
Department of Tumor Cell Biology, St. Jude Children's Research
Hospital, Memphis, Tennessee 38105
We demonstrate the existence of a large endoplasmic reticulum
(ER)-localized multiprotein complex that is comprised of the molecular
chaperones BiP; GRP94; CaBP1; protein disulfide isomerase (PDI); ERdj3,
a recently identified ER Hsp40 cochaperone; cyclophilin B; ERp72;
GRP170; UDP-glucosyltransferase; and SDF2-L1. This complex is
associated with unassembled, incompletely folded immunoglobulin heavy
chains. Except for ERdj3, and to a lesser extent PDI, this complex also
forms in the absence of nascent protein synthesis and is found in a
variety of cell types. Cross-linking studies reveal that the majority
of these chaperones are included in the complex. Our data suggest that
this subset of ER chaperones forms an ER network that can bind to
unfolded protein substrates instead of existing as free pools that
assembled onto substrate proteins. It is noticeable that most of the
components of the calnexin/calreticulin system, which include some of
the most abundant chaperones inside the ER, are either not detected in
this complex or only very poorly represented. This study demonstrates
an organization of ER chaperones and folding enzymes that has not been
previously appreciated and suggests a spatial separation of the two
chaperone systems that may account for the temporal interactions
observed in other studies.
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