Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family

Rebbe, Neil F.; Ware, Jerry; Bertina, Rogier M.; Modrich, Paul; Stafford, Darrel W.

doi:10.1016/0378-1119(87)90012-6

Cited by 199 publications

(120 citation statements)

References 24 publications

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“…The coding sequence for human Hsp90␤ was excised as a SnaBI-SalI fragment from pKN1-3 (Rebbe et al, 1987) and cloned into the SmaI site of pSP64 to add a BamHI site at the 5Ј-end and a SacI site at the 3Ј-end. The BamHI-SacI fragment containing the human HSP90␤ sequence was fused to the GPD promoter in shuttle vector pRS304 (Sikorski and Hieter, 1989) with a 2 replicon.…”

Section: Plasmidsmentioning

confidence: 99%

Hsp90 Is Required for Pheromone Signaling in Yeast

Louvion

Abbas-Terki

Picard

1998

MBoC

107

129

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The heat-shock protein 90 (Hsp90) is a cytosolic molecular chaperone that is highly abundant even at normal temperature. Specific functions for Hsp90 have been proposed based on the characterization of its interactions with certain transcription factors and kinases including Raf in vertebrates and flies. We therefore decided to address the role of Hsp90 for MAP kinase pathways in the budding yeast, an organism amenable to both genetic and biochemical analyses. We found that both basal and induced activities of the pheromone-signaling pathway depend on Hsp90. Signaling is defective in strains expressing low levels or point mutants of yeast Hsp90 (Hsp82), or human Hsp90␤ instead of the wild-type protein. Ste11, a yeast equivalent of Raf, forms complexes with wild-type Hsp90 and depends on Hsp90 function for accumulation. For budding yeast, Ste11 represents the first identified endogenous "substrate" of Hsp90. Moreover, Hsp90 functions in steroid receptor and pheromone signaling can be genetically separated as the Hsp82 point mutant T525I and the human Hsp90␤ are specifically defective for the former and the latter, respectively. These findings further corroborate the view that molecular chaperones must also be considered as transient or stable components of signal transduction pathways. INTRODUCTIONThe 90-kDa heat-shock protein (Hsp90) 1 (for reviews, see Jakob and Buchner, 1994;Csermely et al., 1998) is an ubiquitous and abundantly expressed cytosolic protein even at normal temperature. It is highly conserved from bacteria to mammals. Two genes encode closely related isoforms in mammals as well as in the budding yeast Saccharomyces cerevisiae. Deletion experiments in yeast have shown that the expression of at least one of the two Hsp90 isoforms, either Hsp82 or Hsc82, is essential for viability (Borkovich et al., 1989). Similarly, many mutant alleles of the Drosophila HSP90 homolog, HSP83, are embryonic lethals over a deficiency of the locus (van der Straten et al., 1997), whereas the Escherichia coli homolog of Hsp90, HtpG, appears to be dispensable (Bardwell and Craig, 1988). Hsp90 can act as a molecular chaperone in vitro to promote refolding of denatured proteins (Wiech et al., 1992;Yonehara et al., 1996; see also Shaknovich et al., 1992;Shue and Kohtz, 1994), to hold denatured proteins in a folding-competent state for other chaperones (Freeman and Morimoto, 1996;Yonehara et al., 1996) and to prevent protein unfolding and aggregation (Miyata and Yahara, 1992;Jakob et al., 1995aJakob et al., , 1995bYonehara et al., 1996).The interaction of Hsp90 with steroid receptors, which can be thought of as a signal transduction complex, has been the most extensively investigated. A variety of in vitro and in vivo studies have revealed that steroid receptors are complexed with Hsp90 and several other proteins in the absence of hormone (for review, see Pratt and Toft, 1997). Upon ligand binding, the hormone binding domain (HBD) undergoes a conformational change that results in the release of Hsp90 and the concomitant acti...

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Section: Plasmidsmentioning

confidence: 99%

Hsp90 Is Required for Pheromone Signaling in Yeast

Louvion

Abbas-Terki

Picard

1998

MBoC

107

129

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“…The results presented here demonstrate that sequences within the first intron of the human hsp86 gene (also known as hsp89a; Hickey et al 1989), are responsible for this activation. Intron I is remarkable because of two criteria: first, its position immediately preceding the translation start codon is highly conserved among higher eukaryotes (Hackett & Lis 1983;Hickey et al 1989;Rebbe et al 1989;Vourc'h et al 1989;Walter et al 1989;Moore et al 1990). In contrast, other introns found within the 90 kDa hsp gene family show considerable variation.…”

Section: Discussionmentioning

confidence: 99%

Basal level transcription of the human hsp86 gene is directed by intron‐based elements

1997

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“…Therefore, we have tried to inhibit inductive HSP90 synthesis by using antisense oligonucleotides including the starting codon of human HSP90 (Rebbe et al 1989). Unfortunately, it has not been successful so far because of 1 study of HSPs expression foil owm g the stimulation uncertain reasons.…”

Section: Discussionmentioning

confidence: 99%

Induction of 73-kDa and 90-kDa Heat Shock Protein Expression in HL60 Cells during Differentiation.

Lee¹,

Hirokawa²,

Kitabayashi³

et al. 1995

Tohoku J. Exp. Med.

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We investigated the expression of heat shock proteins HSP73 and HSP90 in human promyelocytic line HL60 during their differentiation induced by phorbor ester and all trans retinoic acid (ATRA). Polyclonal antibodies which had been raised against HSPs purified from bovine brains were used to detect human HSPs. Semiquantitation of HSPs was performed by immunoblotting. Induction of monocytoid and granulocytoid differentiation with phorbor ester and ATRA was accompanied by increased expression of HSP73 and HSP90 with distinct kinetics. Increased expression of both HSPs was confirmed by immunocytochemical studies. Our results suggest that HSP73 and HSP90 may be involved in differentiation of HL60 cells.heat shock proteins; HL60 cells; differentiationHeat shock proteins (HSPs) have been described as a family of proteins expressed in not only prokaryotes but eukaryotes whose production is induced by a variety of noxious insults (Hunt and Morimoto 1985;Burdon 1986;Lindquist 1986). It is now clear that HSPs are also present and active in normal cells and serve important physiological functions (Schlesinger 1986;Ellis 1987;Lindquist and Craig 1988). HSPs have been generally defined by their molecular weight: HSP90, HSP70 and low molecular weight HSP families (Schlesinger 1986;Itoh and Tashima 1990). HSP70 consists of two forms of proteins: the stressinducible 72-kDa protein (HSP72), an induced form whose synthesis is most obvious after physiological stress, and the constitutive 73-kDa protein (HSP73, Welch and Framisco 1985), a constitutively present in appreciable levels under normal condition. HSP90 is constitutively present in mammalian cells and

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Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family

Cited by 199 publications

References 24 publications

Hsp90 Is Required for Pheromone Signaling in Yeast

Hsp90 Is Required for Pheromone Signaling in Yeast

Basal level transcription of the human hsp86 gene is directed by intron‐based elements

Induction of 73-kDa and 90-kDa Heat Shock Protein Expression in HL60 Cells during Differentiation.

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