Unfolded Proteins Are Ire1-Activating Ligands That Directly Induce the Unfolded Protein Response-Reference-Cited by-同舟云学术

Unfolded Proteins Are Ire1-Activating Ligands That Directly Induce the Unfolded Protein Response

Published:2011-09-30 Issue:6051 Volume:333 Page:1891-1894
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Gardner Brooke M.¹,Walter Peter¹²

Affiliation:

1. Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA.

2. Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94158, USA.

Abstract

A newly synthesized secretory protein quality control pathway is activated by direct binding of misfolded proteins to a sensor in the endoplasmic reticulum.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference24 articles.

1. Signal integration in the endoplasmic reticulum unfolded protein response

2. A Novel Mechanism for Regulating Activity of a Transcription Factor That Controls the Unfolded Protein Response

3. The Transmembrane Kinase Ire1p Is a Site-Specific Endonuclease That Initiates mRNA Splicing in the Unfolded Protein Response

4. Endoplasmic Reticulum Stress-induced mRNA Splicing Permits Synthesis of Transcription Factor Hac1p/Ern4p That Activates the Unfolded Protein Response

5. Cloning of mammalian Ire1 reveals diversity in the ER stress responses

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