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Book: Coordinating organismal physiology through the unfolded protein response

Wiseman, R. Luke / Haynes, Cole M.

(Current topics in microbiology and immunology ; volume 414 ; Biomedicine)

2018

Author's details	R. Luke Wiseman, Cole M. Haynes, editors
Series title	Current topics in microbiology and immunology ; volume 414 Biomedicine
Collection
Keywords	endoplasmic reticulum stress ; unfolded protein response signaling ; secretory proteostasis ; neurodegenerative disease ; stress-sensing proteins ; lipid homeostasis ; calcium regulation ; organellar morphology
Subject code	610
Language	English
Size	vii, 213 Seiten, Illustrationen, 23.5 cm x 15.5 cm
Publisher	Springer
Publishing place	Cham, Switzerland
Publishing country	Switzerland
Document type	Book
HBZ-ID	HT019688407
ISBN	978-3-319-78529-5 ; 3-319-78529-X ; 9783319785301 ; 3319785303
Database	Catalogue ZB MED Medicine, Health

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Book ; Online ; E-Book: Coordinating organismal physiology through the unfolded protein response

Wiseman, R. Luke / Haynes, Cole M.

(Current topics in microbiology and immunology ; 414)

2018

Author's details	R. Luke Wiseman, Cole M. Haynes editors
Series title	Current topics in microbiology and immunology ; 414
Collection
Language	English
Size	1 Online-Ressource (vii, 213 Seiten), Illustrationen
Publisher	Springer
Publishing place	Cham
Publishing country	Switzerland
Document type	Book ; Online ; E-Book
Remark	Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
HBZ-ID	HT019704727
ISBN	978-3-319-78530-1 ; 9783319785295 ; 3-319-78530-3 ; 331978529X
DOI	10.1007/978-3-319-78530-1
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Article ; Online: Lining up for quality control: linear ubiquitin and proteotoxicity.

Wiseman, R Luke

The EMBO journal

2019 Volume 38, Issue 9

MeSH term(s)	Proteasome Endopeptidase Complex ; Ubiquitin ; Ubiquitination
Chemical Substances	Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2019-04-11
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.2019101985
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.MG 100: Show issues

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Article ; Online: Mapping stress-responsive signaling pathways induced by mitochondrial proteostasis perturbations.

Madrazo, Nicole / Khattar, Zinia / Powers, Evan T / Rosarda, Jessica D / Wiseman, R Luke

Molecular biology of the cell

2024 Volume 35, Issue 5, Page(s) ar74

Abstract: Imbalances in mitochondrial proteostasis are associated with pathologic mitochondrial dysfunction implicated in etiologically diverse diseases. This has led to considerable interest in defining the mechanisms responsible for regulating mitochondria in ... ...

Abstract	Imbalances in mitochondrial proteostasis are associated with pathologic mitochondrial dysfunction implicated in etiologically diverse diseases. This has led to considerable interest in defining the mechanisms responsible for regulating mitochondria in response to mitochondrial stress. Numerous stress-responsive signaling pathways have been suggested to regulate mitochondria in response to proteotoxic stress. These include the integrated stress response (ISR), the heat shock response (HSR), and the oxidative stress response (OSR). Here, we define the stress signaling pathways activated in response to chronic mitochondrial proteostasis perturbations by monitoring the expression of sets of genes regulated downstream of each of these signaling pathways in published Perturb-seq datasets from K562 cells CRISPRi-depleted of mitochondrial proteostasis factors. Interestingly, we find that the ISR is preferentially activated in response to chronic, genetically-induced mitochondrial proteostasis stress, with no other pathway showing significant activation. Further, we demonstrate that CRISPRi depletion of other mitochondria-localized proteins similarly shows preferential activation of the ISR relative to other stress-responsive signaling pathways. These results both establish our gene set profiling approach as a viable strategy to probe stress responsive signaling pathways induced by perturbations to specific organelles and identify the ISR as the predominant stress-responsive signaling pathway activated in response to chronic disruption of mitochondrial proteostasis.
MeSH term(s)	Proteostasis/physiology ; Mitochondria/metabolism ; Oxidative Stress ; Signal Transduction/physiology ; Heat-Shock Response ; Mitochondrial Proteins/metabolism
Chemical Substances	Mitochondrial Proteins
Language	English
Publishing date	2024-03-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E24-01-0041
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Zs.MO 410: Show issues

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Article: Mapping Stress-Responsive Signaling Pathways Induced by Mitochondrial Proteostasis Perturbations.

Madrazo, Nicole / Khattar, Zinia / Powers, Evan T / Rosarda, Jessica D / Wiseman, R Luke

bioRxiv : the preprint server for biology

2024

Abstract: Imbalances in mitochondrial proteostasis are associated with pathologic mitochondrial dysfunction implicated in etiologically-diverse diseases. This has led to considerable interest in defining the biological mechanisms responsible for regulating ... ...

Abstract	Imbalances in mitochondrial proteostasis are associated with pathologic mitochondrial dysfunction implicated in etiologically-diverse diseases. This has led to considerable interest in defining the biological mechanisms responsible for regulating mitochondria in response to mitochondrial stress. Numerous stress responsive signaling pathways have been suggested to regulate mitochondria in response to proteotoxic stress, including the integrated stress response (ISR), the heat shock response (HSR), and the oxidative stress response (OSR). Here, we define the specific stress signaling pathways activated in response to mitochondrial proteostasis stress by monitoring the expression of sets of genes regulated downstream of each of these signaling pathways in published Perturb-seq datasets from K562 cells CRISPRi-depleted of individual mitochondrial proteostasis factors. Interestingly, we find that the ISR is preferentially activated in response to mitochondrial proteostasis stress, with no other pathway showing significant activation. Further expanding this study, we show that broad depletion of mitochondria-localized proteins similarly shows preferential activation of the ISR relative to other stress-responsive signaling pathways. These results both establish our gene set profiling approach as a viable strategy to probe stress responsive signaling pathways induced by perturbations to specific organelles and identify the ISR as the predominant stress-responsive signaling pathway activated in response to mitochondrial proteostasis disruption.
Language	English
Publishing date	2024-02-01
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.01.30.577830
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Stress-responsive regulation of extracellular proteostasis.

Mesgarzadeh, Jaleh S / Buxbaum, Joel N / Wiseman, R Luke

The Journal of cell biology

2022 Volume 221, Issue 4

Abstract: Genetic, environmental, and aging-related insults can promote the misfolding and subsequent aggregation of secreted proteins implicated in the pathogenesis of numerous diseases. This has led to considerable interest in understanding the molecular ... ...

Abstract	Genetic, environmental, and aging-related insults can promote the misfolding and subsequent aggregation of secreted proteins implicated in the pathogenesis of numerous diseases. This has led to considerable interest in understanding the molecular mechanisms responsible for regulating proteostasis in extracellular environments such as the blood and cerebrospinal fluid (CSF). Extracellular proteostasis is largely dictated by biological pathways comprising chaperones, folding enzymes, and degradation factors localized to the ER and extracellular space. These pathways limit the accumulation of nonnative, potentially aggregation-prone proteins in extracellular environments. Many reviews discuss the molecular mechanisms by which these pathways impact the conformational integrity of the secreted proteome. Here, we instead focus on describing the stress-responsive mechanisms responsible for adapting ER and extracellular proteostasis pathways to protect the secreted proteome from pathologic insults that challenge these environments. Further, we highlight new strategies to identify stress-responsive pathways involved in regulating extracellular proteostasis and describe the pathologic and therapeutic implications for these pathways in human disease.
MeSH term(s)	Animals ; Endoplasmic Reticulum/metabolism ; Extracellular Space/metabolism ; Humans ; Molecular Chaperones/metabolism ; Proteostasis ; Stress, Physiological ; Unfolded Protein Response
Chemical Substances	Molecular Chaperones
Language	English
Publishing date	2022-02-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202112104
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Article ; Online: Reshaping endoplasmic reticulum quality control through the unfolded protein response.

Wiseman, R Luke / Mesgarzadeh, Jaleh S / Hendershot, Linda M

Molecular cell

2022 Volume 82, Issue 8, Page(s) 1477–1491

Abstract: Endoplasmic reticulum quality control (ERQC) pathways comprising chaperones, folding enzymes, and degradation factors ensure the fidelity of ER protein folding and trafficking to downstream secretory environments. However, multiple factors, including ... ...

Abstract	Endoplasmic reticulum quality control (ERQC) pathways comprising chaperones, folding enzymes, and degradation factors ensure the fidelity of ER protein folding and trafficking to downstream secretory environments. However, multiple factors, including tissue-specific secretory proteomes, environmental and genetic insults, and organismal aging, challenge ERQC. Thus, a key question is: how do cells adapt ERQC to match the diverse, ever-changing demands encountered during normal physiology and in disease? The answer lies in the unfolded protein response (UPR), a signaling mechanism activated by ER stress. In mammals, the UPR comprises three signaling pathways regulated downstream of the ER membrane proteins IRE1, ATF6, and PERK. Upon activation, these UPR pathways remodel ERQC to alleviate cellular stress and restore ER function. Here, we describe how UPR signaling pathways adapt ERQC, highlighting their importance for maintaining ER function across tissues and the potential for targeting the UPR to mitigate pathologies associated with protein misfolding diseases.
MeSH term(s)	Animals ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum Stress/genetics ; Mammals ; Quality Control ; Signal Transduction ; Unfolded Protein Response
Language	English
Publishing date	2022-04-21
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2022.03.025
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Starting at the beginning: endoplasmic reticulum proteostasis and systemic amyloid disease.

Romine, Isabelle C / Wiseman, R Luke

The Biochemical journal

2020 Volume 477, Issue 9, Page(s) 1721–1732

Abstract: Systemic amyloid diseases are characterized by the deposition of an amyloidogenic protein as toxic oligomers and amyloid fibrils on tissues distal from the site of protein synthesis. Traditionally, these diseases have been viewed as disorders of ... ...

Abstract	Systemic amyloid diseases are characterized by the deposition of an amyloidogenic protein as toxic oligomers and amyloid fibrils on tissues distal from the site of protein synthesis. Traditionally, these diseases have been viewed as disorders of peripheral target tissues where aggregates are deposited, and toxicity is observed. However, recent evidence highlights an important role for endoplasmic reticulum (ER) proteostasis pathways within tissues synthesizing and secreting amyloidogenic proteins, such as the liver, in the pathogenesis of these disorders. Here, we describe the pathologic implications of ER proteostasis and its regulation on the toxic extracellular aggregation of amyloidogenic proteins implicated in systemic amyloid disease pathogenesis. Furthermore, we discuss the therapeutic potential for targeting ER proteostasis to reduce the secretion and toxic aggregation of amyloidogenic proteins to mitigate peripheral amyloid-associated toxicity involved in the onset and progression of systemic amyloid diseases.
MeSH term(s)	Amyloid/metabolism ; Amyloidogenic Proteins/metabolism ; Amyloidosis/metabolism ; Amyloidosis/pathology ; Animals ; Benzoxazoles/pharmacology ; Drug Development ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum Stress ; Humans ; Prealbumin/metabolism ; Proteostasis ; Unfolded Protein Response
Chemical Substances	Amyloid ; Amyloidogenic Proteins ; Benzoxazoles ; Prealbumin ; TTR protein, human ; tafamidis (8FG9H9D31J)
Language	English
Publishing date	2020-05-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BCJ20190312
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Article ; Online: PERK Signaling Regulates Extracellular Proteostasis of an Amyloidogenic Protein During Endoplasmic Reticulum Stress.

Romine, Isabelle C / Wiseman, R Luke

Scientific reports

2019 Volume 9, Issue 1, Page(s) 410

Abstract: The PERK arm of the unfolded protein response (UPR) regulates cellular proteostasis and survival in response to endoplasmic reticulum (ER) stress. However, the impact of PERK signaling on extracellular proteostasis is poorly understood. We define how ... ...

Abstract	The PERK arm of the unfolded protein response (UPR) regulates cellular proteostasis and survival in response to endoplasmic reticulum (ER) stress. However, the impact of PERK signaling on extracellular proteostasis is poorly understood. We define how PERK signaling influences extracellular proteostasis during ER stress using a conformational reporter of the secreted amyloidogenic protein transthyretin (TTR). We show that inhibiting PERK signaling impairs secretion of destabilized TTR during thapsigargin (Tg)-induced ER stress by increasing its ER retention in chaperone-bound complexes. Interestingly, PERK inhibition increases the ER stress-dependent secretion of TTR in non-native conformations that accumulate extracellularly as soluble oligomers. Pharmacologic or genetic TTR stabilization partially restores secretion of native TTR tetramers. However, PERK inhibition still increases the ER stress-dependent secretion of TTR in non-native conformations under these conditions, indicating that the conformation of stable secreted proteins can also be affected by inhibiting PERK. Our results define a role for PERK in regulating extracellular proteostasis during ER stress and indicate that genetic or aging-related alterations in PERK signaling can exacerbate ER stress-related imbalances in extracellular proteostasis implicated in diverse diseases.
MeSH term(s)	Amyloid Neuropathies, Familial/metabolism ; Amyloid Neuropathies, Familial/pathology ; Endoplasmic Reticulum Stress ; HEK293 Cells ; Humans ; Prealbumin/metabolism ; Proteostasis ; Thapsigargin/adverse effects ; Thapsigargin/pharmacology ; eIF-2 Kinase/genetics ; eIF-2 Kinase/metabolism
Chemical Substances	Prealbumin ; TTR protein, human ; Thapsigargin (67526-95-8) ; EIF2AK3 protein, human (EC 2.7.11.1) ; eIF-2 Kinase (EC 2.7.11.1)
Language	English
Publishing date	2019-01-23
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-018-37207-0
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Cryo-EM structure of hexameric yeast Lon protease (PIM1) highlights the importance of conserved structural elements.

Yang, Jie / Song, Albert S / Wiseman, R Luke / Lander, Gabriel C

The Journal of biological chemistry

2022 Volume 298, Issue 3, Page(s) 101694

Abstract: Lon protease is a conserved ATP-dependent serine protease composed of an AAA+ domain that mechanically unfolds substrates and a serine protease domain that degrades these unfolded substrates. In yeast, dysregulation of Lon protease (PIM1) attenuates ... ...

Abstract	Lon protease is a conserved ATP-dependent serine protease composed of an AAA+ domain that mechanically unfolds substrates and a serine protease domain that degrades these unfolded substrates. In yeast, dysregulation of Lon protease (PIM1) attenuates lifespan and leads to gross mitochondrial morphological perturbations. Although structures of the bacterial and human Lon protease reveal a hexameric assembly, yeast PIM1 was speculated to form a heptameric assembly and is uniquely characterized by a ∼50-residue insertion between the ATPase and protease domains. To further understand the yeast-specific properties of PIM1, we determined a high-resolution cryo-electron microscopy structure of PIM1 in a substrate-translocating state. Here, we reveal that PIM1 forms a hexamer, conserved with that of bacterial and human Lon proteases, wherein the ATPase domains form a canonical closed spiral that enables pore loop residues to translocate substrates to the protease chamber. In the substrate-translocating state, PIM1 protease domains form a planar protease chamber in an active conformation and are uniquely characterized by a ∼15-residue C-terminal extension. These additional C-terminal residues form an α-helix located along the base of the protease domain. Finally, we did not observe density for the yeast-specific insertion between the ATPase and protease domains, likely due to high conformational flexibility. Biochemical studies to investigate the insertion using constructs that truncated or replaced the insertion with a glycine-serine linker suggest that the yeast-specific insertion is dispensable for PIM1's enzymatic function. Altogether, our structural and biochemical studies highlight unique components of PIM1 machinery and demonstrate evolutionary conservation of Lon protease function.
MeSH term(s)	ATP-Dependent Proteases/metabolism ; Adenosine Triphosphatases/metabolism ; Cryoelectron Microscopy ; Humans ; Mitochondrial Proteins/chemistry ; Mitochondrial Proteins/metabolism ; Peptide Hydrolases/metabolism ; Protease La/chemistry ; Protease La/metabolism ; Proto-Oncogene Proteins c-pim-1/chemistry ; Proto-Oncogene Proteins c-pim-1/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Serine Endopeptidases/chemistry ; Serine Endopeptidases/metabolism ; Structure-Activity Relationship
Chemical Substances	Mitochondrial Proteins ; Saccharomyces cerevisiae Proteins ; PIM1 protein, human (EC 2.7.11.1) ; Proto-Oncogene Proteins c-pim-1 (EC 2.7.11.1) ; Peptide Hydrolases (EC 3.4.-) ; ATP-Dependent Proteases (EC 3.4.21.-) ; PIM1 protein, S cerevisiae (EC 3.4.21.-) ; Serine Endopeptidases (EC 3.4.21.-) ; Protease La (EC 3.4.21.53) ; Adenosine Triphosphatases (EC 3.6.1.-)
Language	English
Publishing date	2022-02-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.101694
Database	MEDical Literature Analysis and Retrieval System OnLINE

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