The endoplasmic reticulum HSP40 co‐chaperone ERdj3/DNAJB11 assembles and functions as a tetramer
ERdj3/DNAJB11 is an endoplasmic reticulum (ER)‐targeted HSP40 co‐chaperone that performs multifaceted functions involved in coordinating ER and extracellular proteostasis. Here, we show that ERdj3 assembles into a native tetramer that is distinct from the dimeric structure observed for other HSP40 c...
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| Published in | The EMBO journal Vol. 36; no. 15; pp. 2296 - 2309 |
|---|---|
| Main Authors | , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
01.08.2017
Springer Nature B.V John Wiley and Sons Inc |
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| Online Access | Get full text |
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| Abstract | ERdj3/DNAJB11 is an endoplasmic reticulum (ER)‐targeted HSP40 co‐chaperone that performs multifaceted functions involved in coordinating ER and extracellular proteostasis. Here, we show that ERdj3 assembles into a native tetramer that is distinct from the dimeric structure observed for other HSP40 co‐chaperones. An electron microscopy structural model of full‐length ERdj3 shows that these tetramers are arranged as a dimer of dimers formed by distinct inter‐subunit interactions involving ERdj3 domain II and domain III. Targeted deletion of residues 175‐190 within domain II renders ERdj3 a stable dimer that is folded and efficiently secreted from mammalian cells. This dimeric ERdj3 shows impaired substrate binding both in the ER and extracellular environments and reduced interactions with the ER HSP70 chaperone BiP. Furthermore, we show that overexpression of dimeric ERdj3 exacerbates ER stress‐dependent reductions in the secretion of a destabilized, aggregation‐prone protein and increases its accumulation as soluble oligomers in extracellular environments. These results reveal ERdj3 tetramerization as an important structural framework for ERdj3 functions involved in coordinating ER and extracellular proteostasis in the presence and absence of ER stress.
Synopsis
The HSP40 co‐chaperone ERdj3/DNAJB11 coordinates endoplasmic reticulum (ER) and extracellular proteostasis. Cryo‐EM shows ERdj3 to adopt a native tetramer form that is required for efficient substrate binding and for maintaining secretory proteostasis during ER stress.
The ER HSP40 co‐chaperone ERdj3 assembles into a native tetramer.
Electron microscopy reveals the domain architecture of the ERdj3 tetramer.
Disruption of ERdj3 domain II renders ERdj3 a stable dimer.
Disruption of the ERdj3 tetramer decreases substrate binding.
Dimeric ERdj3 shows impaired capacity to regulate secretory proteostasis during ER stress.
Graphical Abstract
CryoEM reveals that co‐chaperone ERdj3 displays an unusual tetramer organization, which is required for efficient substrate binding and for maintaining secretory proteostasis during ER stress. |
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| AbstractList | ERdj3/DNAJB11 is an endoplasmic reticulum (ER)-targeted HSP40 co-chaperone that performs multifaceted functions involved in coordinating ER and extracellular proteostasis. Here, we show that ERdj3 assembles into a native tetramer that is distinct from the dimeric structure observed for other HSP40 co-chaperones. An electron microscopy structural model of full-length ERdj3 shows that these tetramers are arranged as a dimer of dimers formed by distinct inter-subunit interactions involving ERdj3 domain II and domain III. Targeted deletion of residues 175-190 within domain II renders ERdj3 a stable dimer that is folded and efficiently secreted from mammalian cells. This dimeric ERdj3 shows impaired substrate binding both in the ER and extracellular environments and reduced interactions with the ER HSP70 chaperone BiP. Furthermore, we show that overexpression of dimeric ERdj3 exacerbates ER stress-dependent reductions in the secretion of a destabilized, aggregation-prone protein and increases its accumulation as soluble oligomers in extracellular environments. These results reveal ERdj3 tetramerization as an important structural framework for ERdj3 functions involved in coordinating ER and extracellular proteostasis in the presence and absence of ER stress. Synopsis The HSP40 co-chaperone ERdj3/DNAJB11 coordinates endoplasmic reticulum (ER) and extracellular proteostasis. Cryo-EM shows ERdj3 to adopt a native tetramer form that is required for efficient substrate binding and for maintaining secretory proteostasis during ER stress. The ER HSP40 co-chaperone ERdj3 assembles into a native tetramer. Electron microscopy reveals the domain architecture of the ERdj3 tetramer. Disruption of ERdj3 domain II renders ERdj3 a stable dimer. Disruption of the ERdj3 tetramer decreases substrate binding. Dimeric ERdj3 shows impaired capacity to regulate secretory proteostasis during ER stress. ERdj3/DNAJB11 is an endoplasmic reticulum (ER)-targeted HSP40 co-chaperone that performs multifaceted functions involved in coordinating ER and extracellular proteostasis. Here, we show that ERdj3 assembles into a native tetramer that is distinct from the dimeric structure observed for other HSP40 co-chaperones. An electron microscopy structural model of full-length ERdj3 shows that these tetramers are arranged as a dimer of dimers formed by distinct inter-subunit interactions involving ERdj3 domain II and domain III Targeted deletion of residues 175-190 within domain II renders ERdj3 a stable dimer that is folded and efficiently secreted from mammalian cells. This dimeric ERdj3 shows impaired substrate binding both in the ER and extracellular environments and reduced interactions with the ER HSP70 chaperone BiP. Furthermore, we show that overexpression of dimeric ERdj3 exacerbates ER stress-dependent reductions in the secretion of a destabilized, aggregation-prone protein and increases its accumulation as soluble oligomers in extracellular environments. These results reveal ERdj3 tetramerization as an important structural framework for ERdj3 functions involved in coordinating ER and extracellular proteostasis in the presence and absence of ER stress. ERdj3/DNAJB11 is an endoplasmic reticulum (ER)-targeted HSP40 co-chaperone that performs multifaceted functions involved in coordinating ER and extracellular proteostasis. Here, we show that ERdj3 assembles into a native tetramer that is distinct from the dimeric structure observed for other HSP40 co-chaperones. An electron microscopy structural model of full-length ERdj3 shows that these tetramers are arranged as a dimer of dimers formed by distinct inter-subunit interactions involving ERdj3 domain II and domain III Targeted deletion of residues 175-190 within domain II renders ERdj3 a stable dimer that is folded and efficiently secreted from mammalian cells. This dimeric ERdj3 shows impaired substrate binding both in the ER and extracellular environments and reduced interactions with the ER HSP70 chaperone BiP. Furthermore, we show that overexpression of dimeric ERdj3 exacerbates ER stress-dependent reductions in the secretion of a destabilized, aggregation-prone protein and increases its accumulation as soluble oligomers in extracellular environments. These results reveal ERdj3 tetramerization as an important structural framework for ERdj3 functions involved in coordinating ER and extracellular proteostasis in the presence and absence of ER stress.ERdj3/DNAJB11 is an endoplasmic reticulum (ER)-targeted HSP40 co-chaperone that performs multifaceted functions involved in coordinating ER and extracellular proteostasis. Here, we show that ERdj3 assembles into a native tetramer that is distinct from the dimeric structure observed for other HSP40 co-chaperones. An electron microscopy structural model of full-length ERdj3 shows that these tetramers are arranged as a dimer of dimers formed by distinct inter-subunit interactions involving ERdj3 domain II and domain III Targeted deletion of residues 175-190 within domain II renders ERdj3 a stable dimer that is folded and efficiently secreted from mammalian cells. This dimeric ERdj3 shows impaired substrate binding both in the ER and extracellular environments and reduced interactions with the ER HSP70 chaperone BiP. Furthermore, we show that overexpression of dimeric ERdj3 exacerbates ER stress-dependent reductions in the secretion of a destabilized, aggregation-prone protein and increases its accumulation as soluble oligomers in extracellular environments. These results reveal ERdj3 tetramerization as an important structural framework for ERdj3 functions involved in coordinating ER and extracellular proteostasis in the presence and absence of ER stress. ERdj3/DNAJB11 is an endoplasmic reticulum (ER)‐targeted HSP40 co‐chaperone that performs multifaceted functions involved in coordinating ER and extracellular proteostasis. Here, we show that ERdj3 assembles into a native tetramer that is distinct from the dimeric structure observed for other HSP40 co‐chaperones. An electron microscopy structural model of full‐length ERdj3 shows that these tetramers are arranged as a dimer of dimers formed by distinct inter‐subunit interactions involving ERdj3 domain II and domain III. Targeted deletion of residues 175‐190 within domain II renders ERdj3 a stable dimer that is folded and efficiently secreted from mammalian cells. This dimeric ERdj3 shows impaired substrate binding both in the ER and extracellular environments and reduced interactions with the ER HSP70 chaperone BiP. Furthermore, we show that overexpression of dimeric ERdj3 exacerbates ER stress‐dependent reductions in the secretion of a destabilized, aggregation‐prone protein and increases its accumulation as soluble oligomers in extracellular environments. These results reveal ERdj3 tetramerization as an important structural framework for ERdj3 functions involved in coordinating ER and extracellular proteostasis in the presence and absence of ER stress. Synopsis The HSP40 co‐chaperone ERdj3/DNAJB11 coordinates endoplasmic reticulum (ER) and extracellular proteostasis. Cryo‐EM shows ERdj3 to adopt a native tetramer form that is required for efficient substrate binding and for maintaining secretory proteostasis during ER stress. The ER HSP40 co‐chaperone ERdj3 assembles into a native tetramer. Electron microscopy reveals the domain architecture of the ERdj3 tetramer. Disruption of ERdj3 domain II renders ERdj3 a stable dimer. Disruption of the ERdj3 tetramer decreases substrate binding. Dimeric ERdj3 shows impaired capacity to regulate secretory proteostasis during ER stress. Graphical Abstract CryoEM reveals that co‐chaperone ERdj3 displays an unusual tetramer organization, which is required for efficient substrate binding and for maintaining secretory proteostasis during ER stress. ER dj3/ DNAJB 11 is an endoplasmic reticulum ( ER )‐targeted HSP 40 co‐chaperone that performs multifaceted functions involved in coordinating ER and extracellular proteostasis. Here, we show that ER dj3 assembles into a native tetramer that is distinct from the dimeric structure observed for other HSP 40 co‐chaperones. An electron microscopy structural model of full‐length ER dj3 shows that these tetramers are arranged as a dimer of dimers formed by distinct inter‐subunit interactions involving ER dj3 domain II and domain III . Targeted deletion of residues 175‐190 within domain II renders ER dj3 a stable dimer that is folded and efficiently secreted from mammalian cells. This dimeric ER dj3 shows impaired substrate binding both in the ER and extracellular environments and reduced interactions with the ER HSP 70 chaperone BiP. Furthermore, we show that overexpression of dimeric ER dj3 exacerbates ER stress‐dependent reductions in the secretion of a destabilized, aggregation‐prone protein and increases its accumulation as soluble oligomers in extracellular environments. These results reveal ER dj3 tetramerization as an important structural framework for ER dj3 functions involved in coordinating ER and extracellular proteostasis in the presence and absence of ER stress. ERdj3/DNAJB11 is an endoplasmic reticulum (ER)‐targeted HSP40 co‐chaperone that performs multifaceted functions involved in coordinating ER and extracellular proteostasis. Here, we show that ERdj3 assembles into a native tetramer that is distinct from the dimeric structure observed for other HSP40 co‐chaperones. An electron microscopy structural model of full‐length ERdj3 shows that these tetramers are arranged as a dimer of dimers formed by distinct inter‐subunit interactions involving ERdj3 domain II and domain III. Targeted deletion of residues 175‐190 within domain II renders ERdj3 a stable dimer that is folded and efficiently secreted from mammalian cells. This dimeric ERdj3 shows impaired substrate binding both in the ER and extracellular environments and reduced interactions with the ER HSP70 chaperone BiP. Furthermore, we show that overexpression of dimeric ERdj3 exacerbates ER stress‐dependent reductions in the secretion of a destabilized, aggregation‐prone protein and increases its accumulation as soluble oligomers in extracellular environments. These results reveal ERdj3 tetramerization as an important structural framework for ERdj3 functions involved in coordinating ER and extracellular proteostasis in the presence and absence of ER stress. Synopsis The HSP40 co‐chaperone ERdj3/DNAJB11 coordinates endoplasmic reticulum (ER) and extracellular proteostasis. Cryo‐EM shows ERdj3 to adopt a native tetramer form that is required for efficient substrate binding and for maintaining secretory proteostasis during ER stress. The ER HSP40 co‐chaperone ERdj3 assembles into a native tetramer. Electron microscopy reveals the domain architecture of the ERdj3 tetramer. Disruption of ERdj3 domain II renders ERdj3 a stable dimer. Disruption of the ERdj3 tetramer decreases substrate binding. Dimeric ERdj3 shows impaired capacity to regulate secretory proteostasis during ER stress. CryoEM reveals that co‐chaperone ERdj3 displays an unusual tetramer organization, which is required for efficient substrate binding and for maintaining secretory proteostasis during ER stress. |
| Author | Powers, Evan T Kelly, Jeffery W Chowdhury, Saikat Qu, Song Noxon, Isabelle C Plate, Lars Lander, Gabriel C Chen, Kai‐Chun Wiseman, R Luke Schonhoft, Joseph D |
| AuthorAffiliation | 1 Department of Molecular Medicine The Scripps Research Institute La Jolla CA USA 3 Department of Chemistry The Scripps Research Institute La Jolla CA USA 2 Department of Integrative, Structural, and Computational Biology The Scripps Research Institute La Jolla CA USA 4 Skaggs Institute for Chemical Biology The Scripps Research Institute La Jolla CA USA |
| AuthorAffiliation_xml | – name: 2 Department of Integrative, Structural, and Computational Biology The Scripps Research Institute La Jolla CA USA – name: 3 Department of Chemistry The Scripps Research Institute La Jolla CA USA – name: 1 Department of Molecular Medicine The Scripps Research Institute La Jolla CA USA – name: 4 Skaggs Institute for Chemical Biology The Scripps Research Institute La Jolla CA USA |
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| Keywords | ERdj3/DNAJB11 extracellular chaperone J‐protein co‐chaperone HSP40 secretory proteostasis |
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| Snippet | ERdj3/DNAJB11 is an endoplasmic reticulum (ER)‐targeted HSP40 co‐chaperone that performs multifaceted functions involved in coordinating ER and extracellular... ERdj3/DNAJB11 is an endoplasmic reticulum (ER)-targeted HSP40 co-chaperone that performs multifaceted functions involved in coordinating ER and extracellular... ER dj3/ DNAJB 11 is an endoplasmic reticulum ( ER )‐targeted HSP 40 co‐chaperone that performs multifaceted functions involved in coordinating ER and... |
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| SubjectTerms | Agglomeration Binding Cell Line Chaperones Clonal deletion Dimers Electron microscopy EMBO20 EMBO32 EMBO40 Endoplasmic reticulum Endoplasmic Reticulum - metabolism Epithelial Cells - physiology ERdj3/DNAJB11 extracellular chaperone Gene deletion HSP40 HSP40 Heat-Shock Proteins - metabolism HSP40 Heat-Shock Proteins - ultrastructure Hsp40 protein Hsp70 protein Humans J‐protein co‐chaperone Mammalian cells Microscopy, Electron Oligomers Protein Interaction Mapping Protein Multimerization Secretion secretory proteostasis Stresses Transmission electron microscopy |
| Title | The endoplasmic reticulum HSP40 co‐chaperone ERdj3/DNAJB11 assembles and functions as a tetramer |
| URI | https://link.springer.com/article/10.15252/embj.201695616 https://onlinelibrary.wiley.com/doi/abs/10.15252%2Fembj.201695616 https://www.ncbi.nlm.nih.gov/pubmed/28655754 https://www.proquest.com/docview/1924928519 https://www.proquest.com/docview/1914578610 https://pubmed.ncbi.nlm.nih.gov/PMC5538767 |
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