A 90,000-dalton binding protein common to both steroid receptors and the Rous sarcoma virus transforming protein, pp60v-src.

Schuh, S M; Yonemoto, Wes; Brugge, Joan S.; Bauer, Vickie J.; Riehl, Robert M.; Sullivan, William P.; Toft, David O.

doi:10.1016/s0021-9258(17)38716-1

Cited by 289 publications

(24 citation statements)

References 26 publications

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“…The presence of receptor-associated proteins (including heat shock proteins) has been well established in several systems, although the role of these have not yet been defined. Toft and coworkers have not only shown the association of hsp90 (Schuh et al, 1985) and hsp70 (Kost et al, 1989) with the progesterone receptor, but have also identified several other non-hsp proteins (54, 50 and 23 kDa) associated with the unactivated receptor (Smith et al, 1990). Similarly, a 59 kDa non-receptor protein has been identified as associated with the rabbit uterine progesterone receptor (Tai et al, 1986).…”

Section: Antagonism Between Tcdd and Other Chloroaromatic Compoundsmentioning

confidence: 99%

The Ah receptor and the mechanism of dioxin toxicity

Landers

Bunce

1991

Biochemical Journal

324

127

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Section: Antagonism Between Tcdd and Other Chloroaromatic Compoundsmentioning

confidence: 99%

The Ah receptor and the mechanism of dioxin toxicity

Landers

Bunce

1991

Biochemical Journal

324

127

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“…) Two of the major HSPs, or closely related proteins (termed "HSP cognates"), with molecular masses of 90 and 70 kD are found in normal, unstressed cells where they may play a role in growth control mechanisms. Recent reports have demonstrated the association of HSP 90 with both PP60 .... (31) and with a component of the steroid receptor (5,38). Similarly, members of the HSP 70 family have been reported to associate with P53, a nuclear protein expressed in the G0/G~ transition (34).…”

mentioning

confidence: 92%

Mitogen activation induces the enhanced synthesis of two heat-shock proteins in human lymphocytes.

Haire

Peterson

O’Leary

1988

The Journal of Cell Biology

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Abstract. We have used mitogenic lectin (PHA) and a monoclonal antibody (OKT3) to stimulate human peripheral blood (Go) lymphocytes, in the presence of monocytes, and have found two major preferentially synthesized proteins, 73 and 95 kD, which are induced by the mitogens. The elevated synthesis of both proteins begins ,x,4-6 h after mitogen addition (early to mid G0/G1) before entry into first S phase. Maximum synthesis of both proteins is reached by 12 h after mitogen addition when P95 synthesis represents "~4%, and P73 '~2%, of the total protein synthesis, compared with less than 0.5 % for each protein in cells cultured without mitogen. Thus, the proteins appear to be major components of activated cells. We find that both P73 and P95 are induced by heat stress as well as mitogenic stimulation. The induction of the proteins is not affected by either deleting glucose from the culture media or, alternatively, by supplementing it. Using polyclonal antibodies prepared to each of the proteins isolated from mitogen activated cells and monoclonal antibodies that were raised to heat shock proteins, we are able to show that P95 is electrophoretically and immunologically identical to the HSP 90 induced by heat stress. P73 is one of the 70 kD HSPs, Lymphocytes in the peripheral circulation are, for the most part, in a true (naturally occurring) Go state. The biochemistry of activation after in vitro stimulation of these quiescent cells has been extensively investigated. Mitogen induces departure from Go and transition through G1, a 26-30-h period that is termed the lag phase, before DNA synthesis begins (10). Many of the initial stimulatory events at the cell surface in terms of mitogen binding and subsequent secondary messenger involvement are fairly well understood (47). It is known that during the lag phase, extracellular signals such as mitogens, growth factors and interleukins (9, 44) induce sequential gene expression (15, 35) culminating in DNA synthesis and cell division. The function and identity of many of the gene products appearing in the lag phase are not known. However, it is reasonable to propose that proteins induced by the stimulatory signals in lag phase play an essential role in the onset of DNA synthesis and mitosis (8,11,21). In this paper we present evidence that induction of synthesis of two heat-shock proteins, HSP 90 and HSC 70, occurs in 9 The Rockefeller University Press,

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“…Hsp90 participates in Hsp functioning as repressor of heat shock transcripthe formation of multichaperone complexes that bind tion factor (HSF) could make activation of hsp genes target proteins such as steroid receptors (Catelli et al, dependent on protein unfolding. In a novel in vitro Sanchez et al, 1985;Schuh et al, 1985; Pratt, system, in which human HSF1 can be activated by Nair et al, 1996) and several nonnative protein, heat, and geldanamycin, addition protein kinases. One such multichaperone complex, reof Hsp90 inhibits activation.…”

mentioning

confidence: 99%

Repression of Heat Shock Transcription Factor HSF1 Activation by HSP90 (HSP90 Complex) that Forms a Stress-Sensitive Complex with HSF1

Zou

Guo

Guettouche

et al. 1998

Cell

1,129

912

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Heat shock and other proteotoxic stresses cause accumulation of nonnative proteins that trigger activation of heat shock protein (Hsp) genes. A chaperone/Hsp functioning as repressor of heat shock transcription factor (HSF) could make activation of hsp genes dependent on protein unfolding. In a novel in vitro system, in which human HSF1 can be activated by nonnative protein, heat, and geldanamycin, addition of Hsp90 inhibits activation. Reduction of the level of Hsp90 but not of Hsp/c70, Hop, Hip, p23, CyP40, or Hsp40 dramatically activates HSF1. In vivo, geldanamycin activates HSF1 under conditions in which it is an Hsp90-specific reagent. Hsp90-containing HSF1 complex is present in the unstressed cell and dissociates during stress. We conclude that Hsp90, by itself and/or associated with multichaperone complexes, is a major repressor of HSF1.

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A 90,000-dalton binding protein common to both steroid receptors and the Rous sarcoma virus transforming protein, pp60v-src.

Cited by 289 publications

References 26 publications

The Ah receptor and the mechanism of dioxin toxicity

The Ah receptor and the mechanism of dioxin toxicity

Mitogen activation induces the enhanced synthesis of two heat-shock proteins in human lymphocytes.

Repression of Heat Shock Transcription Factor HSF1 Activation by HSP90 (HSP90 Complex) that Forms a Stress-Sensitive Complex with HSF1

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