The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization

doi:10.1074/jbc.RA117.001294

Title: The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization

Authors:: Wang, Peng; Li, Jingzhi; Tao, Jiahui; Sha, Bingdong

Publication Date:: 2018-01-31

Research Org.:: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Org.:: National Institutes of Health (NIH)

OSTI Identifier:: 1464827

Resource Type:: Journal Article

Journal Name:: Journal of Biological Chemistry

Additional Journal Information:: Journal Volume: 293; Journal Issue: 11; Journal ID: ISSN 0021-9258

Publisher:: American Society for Biochemistry and Molecular Biology

Country of Publication:: United States

Language:: ENGLISH

Citation Formats


                    Wang, Peng, Li, Jingzhi, Tao, Jiahui, and Sha, Bingdong. The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization.  United States: N. p., 2018. 
        Web.  doi:10.1074/jbc.RA117.001294.

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                    Wang, Peng, Li, Jingzhi, Tao, Jiahui, & Sha, Bingdong. The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization.  United States.  doi:10.1074/jbc.RA117.001294.

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                    Wang, Peng, Li, Jingzhi, Tao, Jiahui, and Sha, Bingdong. Wed .  
        "The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization".  United States.  doi:10.1074/jbc.RA117.001294.

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@article{osti_1464827,

  title        = {The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization},

  author       = {Wang, Peng and Li, Jingzhi and Tao, Jiahui and Sha, Bingdong},

  abstractNote = {},

  doi          = {10.1074/jbc.RA117.001294},

  journal      = {Journal of Biological Chemistry},

  issn         = {0021-9258},

  number       = 11,

  volume       = 293,

  place        = {United States},

  year         = {2018},

  month        = {1}

}

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DOI: 10.1074/jbc.RA117.001294

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Title: The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization

Citation Formats

Real-time observation of trigger factor function on translating ribosomes journal, October 2006

Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase journal, January 1999

The Mammalian Unfolded Protein Response journal, June 2005

The Crystal Structure of the Yeast Hsp40 Ydj1 Complexed with Its Peptide Substrate journal, December 2003

The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response journal, September 2006

That which does not kill me makes me stronger: adapting to chronic ER stress journal, October 2007

Two Families of Chaperonin: Physiology and Mechanism journal, November 2007

Structure-based mutagenesis studies of the peptide substrate binding fragment of type I heat-shock protein 40 journal, March 2005

HSP90 at the hub of protein homeostasis: emerging mechanistic insights journal, June 2010

Coot model-building tools for molecular graphics journal, November 2004

Unfolded Proteins Are Ire1-Activating Ligands That Directly Induce the Unfolded Protein Response journal, August 2011

The structure of the PERK kinase domain suggests the mechanism for its activation journal, April 2011

A J-Protein Co-chaperone Recruits BiP to Monomerize IRE1 and Repress the Unfolded Protein Response journal, December 2017

IRE1 Signaling Affects Cell Fate During the Unfolded Protein Response journal, November 2007

The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1 journal, August 2000

Client-Loading Conformation of the Hsp90 Molecular Chaperone Revealed in the Cryo-EM Structure of the Human Hsp90:Hop Complex journal, June 2011

The Crystal Structure of a GroEL/Peptide Complex journal, December 1999

PHENIX: a comprehensive Python-based system for macromolecular structure solution journal, January 2010

On the mechanism of sensing unfolded protein in the endoplasmic reticulum journal, December 2005

Signal integration in the endoplasmic reticulum unfolded protein response journal, July 2007

Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK journal, June 1996

Substrate-Specific Translocational Attenuation during ER Stress Defines a Pre-Emptive Quality Control Pathway journal, December 2006

Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response journal, May 2000

The ER stress sensor PERK luminal domain functions as a molecular chaperone to interact with misfolded proteins journal, November 2016

Coping with stress: eIF2 kinases and translational control journal, January 2006

The impact of the endoplasmic reticulum protein-folding environment on cancer development journal, August 2014

Substrate binding site flexibility of the small heat shock protein molecular chaperones journal, August 2009

Decay of Endoplasmic Reticulum-Localized mRNAs During the Unfolded Protein Response journal, July 2006

Crystal Structure of P58(IPK) TPR Fragment Reveals the Mechanism for its Molecular Chaperone Activity in UPR journal, April 2010

Versatility of Trigger Factor Interactions with Ribosome-Nascent Chain Complexes journal, July 2010

Dimerization and Release of Molecular Chaperone Inhibition Facilitate Activation of Eukaryotic Initiation Factor-2 Kinase in Response to Endoplasmic Reticulum Stress journal, March 2002

Crystal structures reveal transient PERK luminal domain tetramerization in endoplasmic reticulum stress signaling journal, April 2015

The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation journal, November 2011

An unfolded protein-induced conformational switch activates mammalian IRE1 journal, October 2017

Phaser crystallographic software journal, July 2007

Real-time observation of trigger factor function on translating ribosomes
journal, October 2006

Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
journal, January 1999

The Mammalian Unfolded Protein Response
journal, June 2005

The Crystal Structure of the Yeast Hsp40 Ydj1 Complexed with Its Peptide Substrate
journal, December 2003

The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response
journal, September 2006

That which does not kill me makes me stronger: adapting to chronic ER stress
journal, October 2007

Two Families of Chaperonin: Physiology and Mechanism
journal, November 2007

Structure-based mutagenesis studies of the peptide substrate binding fragment of type I heat-shock protein 40
journal, March 2005

HSP90 at the hub of protein homeostasis: emerging mechanistic insights
journal, June 2010

Coot model-building tools for molecular graphics
journal, November 2004

Unfolded Proteins Are Ire1-Activating Ligands That Directly Induce the Unfolded Protein Response
journal, August 2011

The structure of the PERK kinase domain suggests the mechanism for its activation
journal, April 2011

A J-Protein Co-chaperone Recruits BiP to Monomerize IRE1 and Repress the Unfolded Protein Response
journal, December 2017

IRE1 Signaling Affects Cell Fate During the Unfolded Protein Response
journal, November 2007

The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1
journal, August 2000

Client-Loading Conformation of the Hsp90 Molecular Chaperone Revealed in the Cryo-EM Structure of the Human Hsp90:Hop Complex
journal, June 2011

The Crystal Structure of a GroEL/Peptide Complex
journal, December 1999

PHENIX: a comprehensive Python-based system for macromolecular structure solution
journal, January 2010

On the mechanism of sensing unfolded protein in the endoplasmic reticulum
journal, December 2005

Signal integration in the endoplasmic reticulum unfolded protein response
journal, July 2007

Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK
journal, June 1996

Substrate-Specific Translocational Attenuation during ER Stress Defines a Pre-Emptive Quality Control Pathway
journal, December 2006

Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
journal, May 2000

The ER stress sensor PERK luminal domain functions as a molecular chaperone to interact with misfolded proteins
journal, November 2016

Coping with stress: eIF2 kinases and translational control
journal, January 2006

The impact of the endoplasmic reticulum protein-folding environment on cancer development
journal, August 2014

Substrate binding site flexibility of the small heat shock protein molecular chaperones
journal, August 2009

Decay of Endoplasmic Reticulum-Localized mRNAs During the Unfolded Protein Response
journal, July 2006

Crystal Structure of P58(IPK) TPR Fragment Reveals the Mechanism for its Molecular Chaperone Activity in UPR
journal, April 2010

Versatility of Trigger Factor Interactions with Ribosome-Nascent Chain Complexes
journal, July 2010

Dimerization and Release of Molecular Chaperone Inhibition Facilitate Activation of Eukaryotic Initiation Factor-2 Kinase in Response to Endoplasmic Reticulum Stress
journal, March 2002

Crystal structures reveal transient PERK luminal domain tetramerization in endoplasmic reticulum stress signaling
journal, April 2015

The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation
journal, November 2011

An unfolded protein-induced conformational switch activates mammalian IRE1
journal, October 2017

Phaser crystallographic software
journal, July 2007