HSP90 manages the ends

Diane C. DeZwaan, Brian C Freeman

Research output: Contribution to journalReview article

Abstract

The telomere environment requires an efficient means to assemble and disassemble a multitude of structures to operate correctly and to help achieve cellular homeostasis. Telomeres are challenged by a common binding specificity displayed by many of the protein components for telomeric DNA, which could result in competitive DNA interactions, and by a cell cycle-restricted timing of events, which enforces a narrow working period in which to perform numerous tasks. In this review, we discuss how the HSP90 molecular chaperone network avoids these obstacles and facilitates an effective operation of the telomere system.

Original languageEnglish (US)
Pages (from-to)384-391
Number of pages8
JournalTrends in Biochemical Sciences
Volume35
Issue number7
DOIs
StatePublished - Jul 1 2010

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Telomere
Molecular Chaperones
DNA
Cells
Cell Cycle
Homeostasis
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

HSP90 manages the ends. / DeZwaan, Diane C.; Freeman, Brian C.

In: Trends in Biochemical Sciences, Vol. 35, No. 7, 01.07.2010, p. 384-391.

Research output: Contribution to journalReview article

DeZwaan, Diane C. ; Freeman, Brian C. / HSP90 manages the ends. In: Trends in Biochemical Sciences. 2010 ; Vol. 35, No. 7. pp. 384-391.
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