Tunicamycin-inducible polypeptide synthesis during Xenopus laevis embryogenesis

Winning, Robert S.; Bols, Niels C.; Heikkila, John J.

doi:10.1111/j.1432-0436.1991.tb00878.x

Cited by 11 publications

(9 citation statements)

References 35 publications

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“…The antiserum also detected an ϳ78-kDa band compatible with the BiP protein in extracts of the Xenopus kidney cell line A6 (lane 4), but not in extracts of a mammalian cell line (lane 5). As described previously in mammalian and Xenopus cells (17,40), tunicamycin treatment of A6 cells increased the expression of the ϳ78-kDa BiP protein (Fig. 2B, lanes 1 and 2).…”

Section: Characterization Of Xenopusmentioning

confidence: 97%

“…Xenopus laevis is tetraploid, and either co-existence of different alleles or gene duplication could account for these differences. Winning et al (40) have identified three variants of the BiP protein in Xenopus that are expressed in an ordered pattern during embryogenesis. While the significance of multiple BiP proteins in Xenopus remains unknown, our data suggest that they may be due to the expression of more that one BiP gene.…”

Section: Characterization Of Xenopusmentioning

confidence: 99%

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Degradation and Endoplasmic Reticulum Retention of Unassembled α- and β-Subunits of Na,K-ATPase Correlate with Interaction of BiP

Beggah

Mathews

Béguin

et al. 1996

Journal of Biological Chemistry

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Assembly of ␣-and ␤-subunits in the endoplasmic reticulum is a prerequisite for the structural and functional maturation of oligomeric P-type ATPases. In Xenopus oocytes, overexpressed, unassembled ␣-and ␤-subunits of Xenopus Na,K-ATPase are retained in the endoplasmic reticulum (ER) and are degraded with different kinetics, while unassembled ␤-subunits of gastric H,K-ATPase leave the ER. In this study, we have investigated the role of the immunoglobulin-binding protein, BiP, in the folding, assembly, and ER retention of ATPase subunits. We determined the primary sequence of Xenopus BiP and used polyclonal antibodies to examine the interaction with BiP of various wild type and mutant ␣-and ␤-subunits overexpressed in Xenopus oocytes. Our results show that ER-retained, unassembled Na,K-ATPase ␤-subunits, but not transport-competent H,K-ATPase ␤-subunits, efficiently associate with BiP until assembly with ␣-subunits occurs. Furthermore, the kinetics of BiP interaction with unassembled wild type and with mutant Na,K-ATPase ␤-subunits parallels their respective stability against cellular degradation. Finally, ␣-subunits that are overexpressed in oocytes and are rapidly degraded and endogenous oocyte ␣-subunits that are stably expressed as individual assembly-competent proteins also interact with oocyte or exogenous BiP, and the interaction time correlates with the protein's stability. These data demonstrate for the first time that BiP might be involved in a long term maturation arrest and/or in the ER quality control of a multimembrane-spanning protein and lend support for a universal chaperone function of BiP.

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Section: Characterization Of Xenopusmentioning

confidence: 97%

Section: Characterization Of Xenopusmentioning

confidence: 99%

Degradation and Endoplasmic Reticulum Retention of Unassembled α- and β-Subunits of Na,K-ATPase Correlate with Interaction of BiP

Beggah

Mathews

Béguin

et al. 1996

Journal of Biological Chemistry

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“…It is likely that this timing with respect to hsp gene inducibility has been conserved throughout evolution. The expression of a related member of the hsp70 family, namely, glucose-regulated protein 78 (grp78) which is also called immunoglobulin heavy chain binding protein (BiP) has been examined in Xenopus embryos [49]. Grp78 and another glucose-regulated protein, grp98, are abundant within the endoplasmic reticulum and act as chaperones and function in the folding and assembly of new proteins [20,50].…”

Section: Reviewsmentioning

confidence: 99%

“…In Xenopus tissue culture cells as well as in mammalian cells grp78 genes are expressed constitutively but can be induced by inhibitors of glycosylatin, sulfhydryl-reducing compounds and conditions of glucose starvation [50][51][52]. In Xenopus embryos, grp78 and grp78 mRNA are detectable throughout early development including the cleavage stages but their levels are not enhanced by tunicamycin until after the MBT [49]. Furthermore, grp78 genes may be differentially expressed during Xenopus development.…”

Section: Reviewsmentioning

confidence: 99%

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Heat shock protein gene expression during Xenopus development

Heikkila

Ohan

Tam

et al. 1997

CMLS, Cell. mol. life sci.

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Stress-induced heat shock protein gene expression is developmentally regulated during early embryogenesis of the frog, Xenopus laevis. For example, a number of heat shock protein genes, such as hsp70, hsp90, and ubiquitin are not heat-inducible until after the midblastula stage of embryogenesis. Furthermore, the family of small heat shock protein genes, hsp30, are differentially expressed after the midblastula stage as well as being regulated at the level of mRNA stability. Many of these stress proteins are also synthesized constitutively during oogenesis and embryogenesis during which they may act as molecular chaperones as well as being involved in sequestering proteins in an inactive state until required by the developing embryo. Furthermore the induction of these stress protein genes has been correlated with enhanced thermoresistance. During stressful conditions heat shock proteins probably prevent aggregation or misfolding of damaged proteins within the embryo.

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