Interactions of Hsp90 with histones and related peptides

Schnaider, Tamás; Oikarinen, Jouko; Ishiwatari-Hayasaka, Haruko; Yahara, Ichiro; Csermely, Péter

doi:10.1016/s0024-3205(99)00508-1

Cited by 33 publications

(21 citation statements)

References 37 publications

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“…HSP-70, HSP-27, and HSP-90 all are known to promote cell survival through various mechanisms within cells, including stress kinase inhibition (32,33), protection of cells from DNA damage (34,35), modulation of mitochondrial reactive oxygen species production (36), and inhibition of caspase activation (37,38). Thus, maintenance of HSP levels during cold storage may help cells to cope better with reperfusion-associated increases in oxidative stress, mitochondrial disruption, and activation of caspase pathways.…”

Section: Discussionmentioning

confidence: 99%

Heat Shock–Induced Protection of Renal Proximal Tubular Epithelial Cells from Cold Storage and Rewarming Injury

Healy¹,

Daly²,

Docherty³

et al. 2006

Journal of the American Society of Nephrology

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Cold storage and reperfusion injury to transplanted kidneys contributes to increased incidence of delayed graft function and may have a negative impact on graft survival. This study examined the mechanisms by which previous heat shock protects against cell death in an in vitro model of kidney storage. Cold storage is mimicked by incubating human renal proximal tubular epithelial (HK-2) cells in University of Wisconsin solution at 4°C with and without subsequent rewarming. Heat shock was induced by incubation of cells at 42°C for 1 h. Altered protein expression was measured by Western blot, and cell viability and apoptosis were measured by propidium iodide DNA staining using flow cytometry. The specific role of heat-shock protein 70 (HSP-70) was determined both by siRNA knockdown and by stable overexpression approaches. Cold storage and rewarming-induced cell death was associated with decreased expression of HSP-70, HSP-90, HSP-27, and Bcl-2. Previous heat shock significantly reduced HK-2 cell death after cold storage and rewarming and was associated with the maintenance of HSP-70, HSP-27, and Bcl-2 protein levels. Blocking heat stress-induced HSP-70 with siRNA did not significantly block the protective effect of heat stress against cold storage and rewarming cell death; however, overexpression of HSP-70 protected HK-2 cells from this stress. It is concluded that previous heat shock protects HK-2 cells from cold storage and rewarming injury. siRNA inhibition of HSP-70 induction did not block the protective effect of heat shock, indicating that HSP-70 is not essential to the heat stress-induced protective effect reported in this study.

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Section: Discussionmentioning

confidence: 99%

Heat Shock–Induced Protection of Renal Proximal Tubular Epithelial Cells from Cold Storage and Rewarming Injury

Healy¹,

Daly²,

Docherty³

et al. 2006

Journal of the American Society of Nephrology

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“…Hsc70 has been shown to play a critical role in the processing of voltage-gated K ϩ channels involved in the trafficking of axonal protein vesicles and the delivery of these channel-containing vesicles to the cell surface (59). Interestingly, recent studies on the binding domains within the Hsp70 and Hsp90 proteins have shown that there may be charge interactions between the various cargo proteins and chaperones (60,61), suggesting a possible role for the charged lysine residue at position 197 of hIK1 in chaperone-mediate protein trafficking.…”

Section: Discussionmentioning

confidence: 99%

Role of an S4-S5 Linker Lysine in the Trafficking of the Ca2+-activated K+ Channels IK1 and SK3

Jones

Hamilton

Devor

2005

Journal of Biological Chemistry

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We have investigated the role of the S4-S5 linker in the trafficking of the intermediate (human (h) IK1) and small (rat SK3) conductance K ؉ channels using a combination of patch-clamp, protein biochemical, and immunofluorescence-based techniques. We demonstrate that a lysine residue (Lys 197 ) located on the intracellular loop between the S4 and S5 domains is necessary for the correct trafficking of hIK1 to the plasma membrane. Mutation of this residue to either alanine or methionine precluded trafficking of the channel to the membrane, whereas the charge-conserving arginine mutation had no effect on channel localization or function. Immunofluorescence localization demonstrated that the K197A mutation resulted in a channel that was primarily retained in the endoplasmic reticulum, and this could not be rescued by incubation at 27°C. Furthermore, immunoblot analysis revealed that the K197A mutation was overexpressed compared with wild-type hIK1 and that this was due to a greatly diminished rate of channel degradation. Co-immunoprecipitation studies demonstrated that the K197A mutation did not preclude multimer formation. Indeed, the K197A mutation dramatically suppressed expression of wild-type hIK1 at the cell surface. Finally, mutation of this conserved lysine in rat SK3 similarly resulted in a channel that failed to correctly traffic to the plasma membrane. These results are the first to demonstrate a critical role for the S4-S5 linker in the trafficking and/or function of IK and SK channels.The human (h) 3 intermediate conductance Ca 2ϩ -activated K ϩ channel IK1 is a member of the KCNN gene family, which also includes SK1-3, the small conductance Ca 2ϩ -activated K ϩ channels. Within this channel family, there is ϳ40% amino acid sequence homology, with the greatest level of identity occurring in the pore and proximal C terminus, a region known to constitutively bind calmodulin (1, 2), thereby conferring Ca 2ϩ sensitivity to these channels. The hIK1 channel is now known to be the Gardos channel involved in red blood cell volume regulation (3). hIK1 is also known to be involved in the Ca 2ϩ -dependent regulation of Cl Ϫ secretion across intestinal and airway epithelia (4 -8). More recent work has demonstrated that the progression of breast cancer cells through the cell cycle is dependent on membrane hyperpolarization resulting from the activation of hIK1 channels (9). hIK1 has also been shown to play a role in both macrophage activation and T-lymphocyte proliferation (10 -12). The critical role that pharmacological modulation of hIK1 may play has been revealed by the demonstration that blockers of hIK1 reduce the autoimmune response to experimental encephalomyelitis in mice (13), reduce brain edema following traumatic brain injury (14), and prevent restenosis following balloon angioplasty (15). Also, openers have been shown to alter vascular tone and hence may modulate peripheral blood pressure (16,17). A great deal of research has focused on both the biophysical and pharmacological properties of hIK1 (18 -20)...

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“…Drosophila Kc cells were grown in Schneider's Drosophila medium (Invitrogen). A total of 3 ϫ 10 6 /ml cells per well in a 6-well plate were seeded 1 day before drug treatment and treated with different concentrations (3,5,10,20,40, and 80 M) of radicicol dissolved in DMSO (Alomone labs) (Fig. 2 A and data not shown) for 4 h. The Kc cells treated with equivalent amounts of DMSO vehicle were used as mock-treated cells.…”

Section: Dna Construct and Generation Of Transgenic Flies Pcr-amplifiedmentioning

confidence: 99%

“…Interaction between Hsp90 and histone proteins led to the suggestion that Hsp90 may affect chromatin structure and organization (5,6). Importantly, involvement of Hsp90 in the disassembly of transcriptional regulatory complexes (2) revealed a potential molecular link between Hsp90 and gene regulation at the chromatin level.…”

mentioning

confidence: 99%

Trithorax requires Hsp90 for maintenance of active chromatin at sites of gene expression

Tariq

Nussbaumer

Chen

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

115

133

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Interactions of Hsp90 with histones and related peptides

Cited by 33 publications

References 37 publications

Heat Shock–Induced Protection of Renal Proximal Tubular Epithelial Cells from Cold Storage and Rewarming Injury

Heat Shock–Induced Protection of Renal Proximal Tubular Epithelial Cells from Cold Storage and Rewarming Injury

Role of an S4-S5 Linker Lysine in the Trafficking of the Ca2+-activated K+ Channels IK1 and SK3

Trithorax requires Hsp90 for maintenance of active chromatin at sites of gene expression

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