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(Received for publication, July 22, 1996, and in revised form, October 30, 1996)
From the BiP/GRP78 is a lumenal stress protein of the
endoplasmic reticulum (ER) that interacts with polypeptide folding
intermediates transiting the secretory compartment. We have studied the
secretion and the stress response in Chinese hamster ovary (CHO) cells
that overexpress either wild-type immunoglobulin binding protein (BiP) or a BiP deletion molecule (residues 175-201) that can bind peptides and ATP but is defective in ATP hydrolysis and concomitant peptide release. Overexpressed wild-type BiP was localized to the ER and unique
vesicles within the nucleus, whereas overexpressed ATPase-defective BiP
was localized to the ER and cytoplasmic vesicles but was absent from
the nucleus. Compared with wild-type CHO cells, overexpression of
ATPase-defective BiP prevented secretion of factor VIII, a coagulation
factor that extensively binds BiP in the lumen of the ER. Under these
conditions factor VIII was stably associated with the ATPase-defective
BiP. In contrast, the secretion of monocyte/macrophage colony
stimulating factor, a protein that is not detected in association with
BiP, was not affected by overexpression of ATPase-defective BiP. These
results show that BiP function is not required for secretion of some
proteins and suggest that some proteins do not interact with BiP upon
transport through the ER.
The presence of unfolded protein in the ER induces transcription of BiP
and also elicits a general inhibition of protein synthesis. Overexpression of wild-type BiP prevented the stress-mediated transcriptional induction of BiP in response to either calcium ionophore A23187 treatment or tunicamycin treatment. In contrast, overexpression of ATPase-defective BiP did not prevent the stress induction of BiP, showing that the ATPase activity is required to
inhibit transcriptional induction. Overexpression of wild-type BiP, but not ATPase-defective BiP, increased survival of cells treated with A23187. The increased survival mediated by overexpressed wild-type BiP correlated with reduced translation inhibition in response to the stress condition. These results indicate that overexpressed BiP alleviated the stress in the ER to prevent BiP transcriptional induction and permit continued translation of cellular
mRNAs.
Volume 272, Number 7,
Issue of February 14, 1997
pp. 4327-4334
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
and§
Howard Hughes Medical Institute, the
§ Department of Biological Chemistry, and the
Department of Anatomy and Cell Biology, University of Michigan
Medical Center, Ann Arbor, Michigan 48109, the ** Genetics Institute
Incorporated, Cambridge, Massachusetts 02140; and the
Department of Tumor Cell Biology, St. Jude
Children's Research Hospital, Memphis, Tennessee 38105
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W. Tirasophon, A. A. Welihinda, and R. J. Kaufman A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells Genes & Dev., June 15, 1998; 12(12): 1812 - 1824. [Abstract] [Full Text]
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H. Liu, E. Miller, B. van de Water, and J. L. Stevens Endoplasmic Reticulum Stress Proteins Block Oxidant-induced Ca2+ Increases and Cell Death J. Biol. Chem., May 22, 1998; 273(21): 12858 - 12862. [Abstract] [Full Text] [PDF]
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