title: ER stress response, peroxisome proliferation, mitochondrial unfolded protein response and Golgi stress response.
abstract: The endoplasmic reticulum (ER) response has been thought a cytoprotective mechanism to cope with accumulation of unfolded proteins in the ER. Recent progress has made a quantum leap revealing that ER stress response can be regarded as an autoregulatory system adjusting the ER capacity to cellular demand. This Copernican change raised a novel fundamental question in cell biology: how do cells regulate the capacity of each organelle in accordance with cellular needs? Although this fundamental question has not been fully addressed yet, research about each organelle has been advancing. The proliferation of the peroxisome is regulated by the PPAR alpha pathway, whereas the abundance of mitochondria appears to be regulated by mitochondrial retrograde signaling and the mitochondrial unfolded protein response. The functional capacity of the Golgi apparatus may be regulated by the mechanism of the Golgi stress response. These observations strongly suggest the existence of an elaborate network of organelle autoregulation in eukaryotic cells.
authors.affiliation: Department of Biophysics, Graduate School of Science, Kyoto University, Japan. hide@biophysics.mbox.media.kyoto-u.ac.jp
authors.forename: Hiderou
authors.initials: H
authors.lastname: Yoshida
mesh_terms: D004721:Endoplasmic Reticulum / Q000502:physiology*; D006056:Golgi Apparatus / Q000502:physiology*; D008928:Mitochondria / Q000502:physiology*; D020675:Peroxisomes / Q000502:physiology*; D011489:Protein Denaturation; D015398:Signal Transduction