The nucleotide sequence encoding the hamster 78-kDa glucose-regulated protein (GRP78) and its conservation between hamster and rat

Ting, Jerry; Wooden, Scott K.; Krizv, Ronald; Kelleher, Kerry; Kaufman, Randal J.; Lee, Amy

doi:10.1016/0378-1119(87)90258-7

Cited by 92 publications

(48 citation statements)

References 12 publications

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“…A 0.5-kb BamHI-XhoI fragment from the BS-mIRE1␣ targeting vector or a 3.6-kb EcoRI-XbaI fragment from pED-hIRE1␣ cDNA was used for Southern and Northern analysis, respectively. The probes for Northern analysis of mXBP1, BiP, and GRP94 were a 0.94-kb XhoI fragment of pcDNA-mXBP1-u, the EcoRI-PstI fragment of hamster BiP (Ting et al 1987), and a 146-bp PCR fragment of mouse GRP94 (142-287 of the coding region), respectively.…”

Section: Southern and Northern Blot Analysismentioning

confidence: 99%

IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response

Lee¹,

Tirasophon²,

Shen³

et al. 2002

Genes Dev.

Self Cite

968

810

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All eukaryotic cells respond to the accumulation of unfolded proteins in the endoplasmic reticulum (ER) by signaling an adaptive pathway termed the unfolded protein response (UPR). In yeast, a type-I ER transmembrane protein kinase, Ire1p, is the proximal sensor of unfolded proteins in the ER lumen that initiates an unconventional splicing reaction on HAC1 mRNA. Hac1p is a transcription factor required for induction of UPR genes. In higher eukaryotic cells, the UPR also induces site-2 protease (S2P)-mediated cleavage of ER-localized ATF6 to generate an N-terminal fragment that activates transcription of UPR genes. To elucidate the requirements for IRE1␣ and ATF6 for signaling the mammalian UPR, we identified a UPR reporter gene that was defective for induction in IRE1␣-null mouse embryonic fibroblasts and S2P-deficient Chinese hamster ovary (CHO) cells. We show that the endoribonuclease activity of IRE1␣ is required to splice XBP1 (X-box binding protein) mRNA to generate a new C terminus, thereby converting it into a potent UPR transcriptional activator. IRE1␣ was not required for ATF6 cleavage, nuclear translocation, or transcriptional activation. However, ATF6 cleavage was required for IRE1␣-dependent induction of UPR transcription. We propose that nuclear-localized IRE1␣ and cytoplasmic-localized ATF6 signaling pathways merge through regulation of XBP1 activity to induce downstream gene expression. Whereas ATF6 increases the amount of XBP1 mRNA, IRE1␣ removes an unconventional 26-nucleotide intron that increases XBP1 transactivation potential. Both processing of ATF6 and IRE1␣-mediated splicing of XBP1 mRNA are required for full activation of the UPR.

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Section: Southern and Northern Blot Analysismentioning

confidence: 99%

IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response

Lee¹,

Tirasophon²,

Shen³

et al. 2002

Genes Dev.

Self Cite

968

810

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“…Drosophila Bip signal peptide (Bip-sp) and honeybee melittin signal peptide (HBM-sp), which are popular secretion signals for the mass production of secretory proteins in insect cells, served as the controls for quantitative comparison [16,17]. Bip is an abundant and highly conserved eukaryotic protein found in the ER lumen, and melittin is a principal component of honeybee toxin (Table 2) [18][19][20][21][22]. The other two signal peptides from endogenous secretory proteins, 30K Da protein (30K-sp) and storage protein 2 (SP2-sp), were employed because of their highest concentrations in silkworm hemolymph.…”

Section: Signal Peptides Used For Secretion In the Baculovirus-silkwomentioning

confidence: 99%

Comparison of signal peptides for efficient protein secretion in the baculovirus-silkworm system

et al. 2013

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The baculovirus-silkworm expression system is widely used as a mass production system for recombinant secretory proteins. However, the final yields of some recombinant proteins are not sufficient for industrial use. In this study, we focused on the signal peptide as a key factor for improving the efficiency of protein production. Endoplasmic reticulum (ER) translocation of newly synthesized proteins is the first stage of the secretion pathway; therefore, the selection of an efficient signal peptide would lead to the efficient secretion of recombinant proteins. The Drosophila Bip and honeybee melittin signal peptides have often been used in this system, but to the best of our knowledge, there has been no study comparing secretion efficiency between exogenous and endogenous signal peptides. In this study we employed signal peptides from 30K Da and SP2 proteins as endogenous signals, and compared secretion efficiency with those of exogenous or synthetic origins. We have found that the endogenous secretory signal from the 30K Da protein is the most efficient for recombinant secretory protein production in the baculovirus-silkworm expression system.

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“…In Figure 3, a comparison of the amino acid sequences of one of the members of tobacco BiP (BLP4), a plant heat shock protein (petunia hsp70, Winter et al, 1988), hamster BiP (Ting et al, 1987), and yeast BiP (Normington et al, 1989;Rose et al, 1989) shows that tobacco BiP is most related to mammalian BiP.…”

Section: Cdna Cloning and Structural Analysismentioning

confidence: 99%

“…They have a highly conserved N-terminal ATP binding domain and a more variable protein binding domain (Flaherty et al, 1990). The luminal binding protein (BiP), identified in various mammals (Munro and Pelham, 1986;Ting et al, 1987;Haas and Meo, 1988;Wooden et al, 1988) and yeasts (Normington et al, 1989;Rose et al, 1989), is a member of the hsp70 family that accomplishes its function in the lumen of the endoplasmic reticulum (ER). BiP differs from the other family members in the presence of an N-terminal signal sequence that is ' Current address: Department of Molecular Genetics, Swedish University of Agricultura1 Sciences, S-750 07 Uppsala, Sweden.…”

Section: Introductionmentioning

confidence: 99%

The tobacco luminal binding protein is encoded by a multigene family.

et al. 1991

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The nucleotide sequence encoding the hamster 78-kDa glucose-regulated protein (GRP78) and its conservation between hamster and rat

Cited by 92 publications

References 12 publications

IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response

IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response

Comparison of signal peptides for efficient protein secretion in the baculovirus-silkworm system

The tobacco luminal binding protein is encoded by a multigene family.

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