Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones

By T. Yoneda, C. Benedetti, F. Urano, S. G. Clark, H. Harding, D. Ron. Journal of Cell Science, 2004

651 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Multi-omics analysis identifies ATF4 as a key regulator of the mitochondrial stress response in mammals (2017, background): “Surprisingly, under the conditions used, we did not detect activation of the prototypical UPRmt, which is generally characterized by the induction of the chaperones HSP60 and HSP10 and the protease CLPP, among others, and which has been mainly described in invertebrates and cellular models as the pr”
Mitochondria: In Sickness and in Health (2012, background): “UPRmt originates in mitochondria from the accumulation of unassembled respiratory complex subunits and is communicated to the nucleus via an unknown mechanism where it culminates in the regulated expression of mitochondrial protein chaperones, such as HSP-60 (Benedetti et al., 2006; Haynes et al., 2”
The NAD+/sirtuin pathway modulates longevity through activation of mitochondrial UPR and FOXO signaling (2013, positive): “H) The NAD+ precursor NR (E and G; 1 mM) and the PARP inhibitor AZD2281 (F and H; 1 mM) induce UPRmt, as evidenced by CLPP expression, in a timedependent fashion in AML12 cells.”
The Cell Non-Autonomous Nature of Electron Transport Chain-Mediated Longevity (2011, positive): “Furthermore, markers of the UPR mt , namely hsp-6p::GFP, have their greatest activation late in larval development at the L4 stage when challenged with mitochondrial stress (Yoneda et al., 2004 ).”