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Science 3 January 1997: Vol. 275. no. 5296, pp. 86 - 88 DOI: 10.1126/science.275.5296.86
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Reports
Interaction of the Thiol-Dependent Reductase ERp57 with
Nascent Glycoproteins
Jason D. Oliver,
Fimme J. van der Wal,
Neil J. Bulleid,
Stephen High
*
Calnexin and calreticulin interact specifically with newly
synthesized glycoproteins in the endoplasmic reticulum (ER) and function as molecular chaperones. The carbohydrate-specific
interactions between ER components and glycoproteins synthesized in
isolated canine pancreatic microsomes were analyzed using a
cross-linking approach. A carbohydrate-dependent interaction between
newly synthesized glycoproteins, the thiol-dependent reductase ERp57,
and either calnexin or calreticulin was identified. The interaction
between ERp57 and the newly synthesized glycoproteins required trimming of the N-linked oligosaccharide side chain. Thus, it is likely that
ERp57 functions as part of the glycoprotein-specific quality control
machinery operating in the lumen of the ER.
School of Biological Sciences, University of Manchester, 2.205 Stopford Building, Oxford Road, Manchester M13 9PT, UK.
*
To whom correspondence should be addressed. E-mail:
shigh{at}fs2.scg.man.ac.uk
Read the Full Text
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- Domains b' and a' of Protein Disulfide Isomerase Fulfill the Minimum Requirement for Function as a Subunit of Prolyl 4-Hydroxylase. THE N-TERMINAL DOMAINS a AND b ENHANCE THIS FUNCTION AND CAN BE SUBSTITUTED IN PART BY THOSE OF ERp57.
- A. Pirneskoski, L. W. Ruddock, P. Klappa, R. B. Freedman, K. I. Kivirikko, and P. Koivunen (2001)
J. Biol. Chem.
276, 11287-11293
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- TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain.
- E.-M. Frickel, R. Riek, I. Jelesarov, A. Helenius, K. Wuthrich, and L. Ellgaard (2002)
PNAS
99, 1954-1959
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- NMR structure of the calreticulin P-domain.
- L. Ellgaard, R. Riek, T. Herrmann, P. Guntert, D. Braun, A. Helenius, and K. Wuthrich (2001)
PNAS
98, 3133-3138
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