DOI: 10.1126/science.274.5293.1713. A Cyclophilin Function in Hsp90-Dependent Signal Transduction

A Cyclophilin Function in Hsp90-Dependent Signal Transduction

10.1126/science.274.5293.1713

Crossref journal-article

American Association for the Advancement of Science (AAAS)

Science (221)

Abstract

Cpr6 and Cpr7, the Saccharomyces cerevisiae homologs of cyclophilin-40 (CyP-40), were shown to form complexes with Hsp90, a protein chaperone that functions in several signal transduction pathways. Deletion of CPR7 caused severe growth defects when combined with mutations that decrease the amount of Hsp90 or Sti1, another component of the Hsp90 chaperone machinery. The activities of two heterologous Hsp90-dependent signal transducers expressed in yeast, glucocorticoid receptor and pp60 v− src kinase, were adversely affected by cpr7 null mutations. These results suggest that CyP-40 cyclophilins play a general role in Hsp90-dependent signal transduction pathways under normal growth conditions.

Bibliography

Duina, A. A., Chang, H.-C. J., Marsh, J. A., Lindquist, S., & Gaber, R. F. (1996). A Cyclophilin Function in Hsp90-Dependent Signal Transduction. Science, 274(5293), 1713â1715.

Authors 5

Andrea A. Duina (first)
Hui-Chen Jane Chang (additional)
James A. Marsh (additional)
Susan Lindquist (additional)
Richard F. Gaber (additional)

References 36 Referenced 172

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Freeman B. C. Toft D. O. Morimoto R. I. Science 274 XXX (1996). (10.1126/science.274.5293.1718)

Dates

Type	When
Created	23 years, 1 month ago (July 27, 2002, 5:45 a.m.)
Deposited	1 year ago (Aug. 7, 2024, 7:41 a.m.)
Indexed	3 weeks, 3 days ago (Aug. 7, 2025, 4:35 p.m.)
Issued	28 years, 8 months ago (Dec. 6, 1996)
Published	28 years, 8 months ago (Dec. 6, 1996)
Published Print	28 years, 8 months ago (Dec. 6, 1996)

Funders 0

None

BibTeX

@article{Duina_1996, title={A Cyclophilin Function in Hsp90-Dependent Signal Transduction}, volume={274}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.274.5293.1713}, DOI={10.1126/science.274.5293.1713}, number={5293}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Duina, Andrea A. and Chang, Hui-Chen Jane and Marsh, James A. and Lindquist, Susan and Gaber, Richard F.}, year={1996}, month=dec, pages={1713–1715} }

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  "abstract": "<jats:p>\n            Cpr6 and Cpr7, the\n            <jats:italic>Saccharomyces cerevisiae</jats:italic>\n            homologs of cyclophilin-40 (CyP-40), were shown to form complexes with Hsp90, a protein chaperone that functions in several signal transduction pathways. Deletion of\n            <jats:italic>CPR7</jats:italic>\n            caused severe growth defects when combined with mutations that decrease the amount of Hsp90 or Sti1, another component of the Hsp90 chaperone machinery. The activities of two heterologous Hsp90-dependent signal transducers expressed in yeast, glucocorticoid receptor and pp60\n            <jats:sup>v\u2212</jats:sup>\n            <jats:sup>\n              <jats:italic>src</jats:italic>\n            </jats:sup>\n            kinase, were adversely affected by\n            <jats:italic>cpr7</jats:italic>\n            null mutations. These results suggest that CyP-40 cyclophilins play a general role in Hsp90-dependent signal transduction pathways under normal growth conditions.\n          </jats:p>",
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  "ISSN": [
    "0036-8075",
    "1095-9203"
  ],
  "subject": [],
  "container-title-short": "Science",
  "published": {
    "date-parts": [
      [
        1996,
        12,
        6
      ]
    ]
  }
}