Literature DB >> 17387279

Unfolded protein response in Drosophila: why another model can make it fly.

Hyung Don Ryoo1, Hermann Steller.   

Abstract

The unfolded protein response (UPR) is an intracellular signaling pathway that is activated in response to stress in the endoplasmic reticulum (ER). UPR can effectively cope with stress by reducing the amount of misfolded protein overload in this subcellular organelle. Significantly, ER-stress is associated with various neurodegenerative disorders, diabetes and cancer, where UPR affects the course of disease manifestation in many cases. While significant progress has been made in various experimental systems over the years, suitable models for in vivo analyses of UPR and disease remain scarce. In this regard, recent developments of Drosophila markers and genetic tools for UPR studies provide powerful means to investigate the connection between UPR and disease in vivo. Here, we review the molecular components of the Drosophila UPR as well as the disease models that may be affected by this signaling pathway.

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Year:  2007        PMID: 17387279     DOI: 10.4161/cc.6.7.4064

Source DB:  PubMed          Journal:  Cell Cycle        ISSN: 1551-4005            Impact factor:   4.534


  25 in total

1.  ER stress inhibits neuronal death by promoting autophagy.

Authors:  Antoine Fouillet; Clemence Levet; Angelique Virgone; Marion Robin; Pierre Dourlen; Jennifer Rieusset; Elise Belaidi; Michel Ovize; Monique Touret; Serge Nataf; Bertrand Mollereau
Journal:  Autophagy       Date:  2012-06-01       Impact factor: 16.016

2.  ER stress protects from retinal degeneration.

Authors:  César S Mendes; Clémence Levet; Gilles Chatelain; Pierre Dourlen; Antoine Fouillet; Marie-Laure Dichtel-Danjoy; Alexis Gambis; Hyung Don Ryoo; Hermann Steller; Bertrand Mollereau
Journal:  EMBO J       Date:  2009-04-02       Impact factor: 11.598

3.  Getting the better of ER stress.

Authors:  Bertrand Mollereau; Serge Manié; Francesco Napoletano
Journal:  J Cell Commun Signal       Date:  2014-10-30       Impact factor: 5.782

4.  A modified UPR stress sensing system reveals a novel tissue distribution of IRE1/XBP1 activity during normal Drosophila development.

Authors:  Michio Sone; Xiaomei Zeng; Joseph Larese; Hyung Don Ryoo
Journal:  Cell Stress Chaperones       Date:  2012-11-17       Impact factor: 3.667

5.  The PERK pathway independently triggers apoptosis and a Rac1/Slpr/JNK/Dilp8 signaling favoring tissue homeostasis in a chronic ER stress Drosophila model.

Authors:  Y Demay; J Perochon; S Szuplewski; B Mignotte; S Gaumer
Journal:  Cell Death Dis       Date:  2014-10-09       Impact factor: 8.469

6.  Loss of Drosophila i-AAA protease, dYME1L, causes abnormal mitochondria and apoptotic degeneration.

Authors:  Y Qi; H Liu; M P Daniels; G Zhang; H Xu
Journal:  Cell Death Differ       Date:  2015-07-10       Impact factor: 15.828

7.  Transcriptional regulation by CHIP/LDB complexes.

Authors:  Revital Bronstein; Liron Levkovitz; Nir Yosef; Michaela Yanku; Eytan Ruppin; Roded Sharan; Heiner Westphal; Brian Oliver; Daniel Segal
Journal:  PLoS Genet       Date:  2010-08-12       Impact factor: 5.917

8.  A Drosophila gain-of-function screen for candidate genes involved in steroid-dependent neuroendocrine cell remodeling.

Authors:  Tao Zhao; Tingting Gu; Heather C Rice; Kathleen L McAdams; Kimberly M Roark; Kaylan Lawson; Sebastien A Gauthier; Kathleen L Reagan; Randall S Hewes
Journal:  Genetics       Date:  2008-02-01       Impact factor: 4.562

9.  Characterization of the properties of a novel mutation in VAPB in familial amyotrophic lateral sclerosis.

Authors:  Han-Jou Chen; Georgia Anagnostou; Andrea Chai; James Withers; Alex Morris; Jason Adhikaree; Giuseppa Pennetta; Jackie S de Belleroche
Journal:  J Biol Chem       Date:  2010-10-12       Impact factor: 5.157

10.  Hyung Don Ryoo: a healthy career in cellular death.

Authors:  Hyung Don Ryoo
Journal:  J Cell Biol       Date:  2009-06-01       Impact factor: 10.539

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