Improved calcium sensor GCaMP-X overcomes the calcium channel perturbations induced by the calmodulin in GCaMP

GCaMP, one popular type of genetically-encoded Ca 2+ indicator, has been associated with various side-effects. Here we unveil the intrinsic problem prevailing over different versions and applications, showing that GCaMP containing CaM (calmodulin) interferes with both gating and signaling of L-type...

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Vydáno v:Nature communications Ročník 9; číslo 1; s. 1504 - 18
Hlavní autoři: Yang, Yaxiong, Liu, Nan, He, Yuanyuan, Liu, Yuxia, Ge, Lin, Zou, Linzhi, Song, Sen, Xiong, Wei, Liu, Xiaodong
Médium: Journal Article
Jazyk:angličtina
Vydáno: London Nature Publishing Group UK 17.04.2018
Nature Publishing Group
Nature Portfolio
Témata:
14/1
14/19
14/34
14/35
14/63
42/109
631/1647/245/2225
631/378/2586
631/45/269/1146
631/80/86/1999
631/80/86/2372
9/10
9/74
96/95
Animals
Biosensing Techniques - methods
Calcium - chemistry
Calcium - metabolism
Calcium channels
Calcium channels (L-type)
Calcium channels (voltage-gated)
Calcium Channels, L-Type - metabolism
Calcium imaging
Calcium ions
Calcium Signaling
Calcium signalling
Calcium-binding protein
Calmodulin
Calmodulin - chemistry
Calmodulin - genetics
Calmodulin - metabolism
Channel gating
Coupling (molecular)
Fluorescent Dyes - chemistry
Gene expression
Genetic Engineering - methods
Green Fluorescent Proteins - chemistry
Green Fluorescent Proteins - genetics
HEK293 Cells
Humanities and Social Sciences
Humans
Intravital Microscopy - methods
Ion Channel Gating
Mice
Mice, Inbred ICR
Molecular Imaging - methods
Morphogenesis
multidisciplinary
Neurons
Patch-Clamp Techniques
Primary Cell Culture
Protein Binding
Science
Science (multidisciplinary)
Side effects
Transcription
ISSN:2041-1723, 2041-1723
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Abstract GCaMP, one popular type of genetically-encoded Ca 2+ indicator, has been associated with various side-effects. Here we unveil the intrinsic problem prevailing over different versions and applications, showing that GCaMP containing CaM (calmodulin) interferes with both gating and signaling of L-type calcium channels (Ca V 1). GCaMP acts as an impaired apoCaM and Ca 2+ /CaM, both critical to Ca V 1, which disrupts Ca 2+ dynamics and gene expression. We then design and implement GCaMP-X, by incorporating an extra apoCaM-binding motif, effectively protecting Ca V 1-dependent excitation–transcription coupling from perturbations. GCaMP-X resolves the problems of detrimental nuclear accumulation, acute and chronic Ca 2+ dysregulation, and aberrant transcription signaling and cell morphogenesis, while still demonstrating excellent Ca 2+ -sensing characteristics partly inherited from GCaMP. In summary, CaM/Ca V 1 gating and signaling mechanisms are elucidated for GCaMP side-effects, while allowing the development of GCaMP-X to appropriately monitor cytosolic, submembrane or nuclear Ca 2+ , which is also expected to guide the future design of CaM-based molecular tools. The popular genetically-encoded Ca 2+ indicator, GCaMP, has several side-effects. Here the authors show that GCaMP containing CaM interferes with gating and signaling of L-type calcium channels, which disrupts Ca 2+ dynamics and gene expression, and develop GCaMP-X to overcome these limitations.
AbstractList GCaMP, one popular type of genetically-encoded Ca 2+ indicator, has been associated with various side-effects. Here we unveil the intrinsic problem prevailing over different versions and applications, showing that GCaMP containing CaM (calmodulin) interferes with both gating and signaling of L-type calcium channels (Ca V 1). GCaMP acts as an impaired apoCaM and Ca 2+ /CaM, both critical to Ca V 1, which disrupts Ca 2+ dynamics and gene expression. We then design and implement GCaMP-X, by incorporating an extra apoCaM-binding motif, effectively protecting Ca V 1-dependent excitation–transcription coupling from perturbations. GCaMP-X resolves the problems of detrimental nuclear accumulation, acute and chronic Ca 2+ dysregulation, and aberrant transcription signaling and cell morphogenesis, while still demonstrating excellent Ca 2+ -sensing characteristics partly inherited from GCaMP. In summary, CaM/Ca V 1 gating and signaling mechanisms are elucidated for GCaMP side-effects, while allowing the development of GCaMP-X to appropriately monitor cytosolic, submembrane or nuclear Ca 2+ , which is also expected to guide the future design of CaM-based molecular tools. The popular genetically-encoded Ca 2+ indicator, GCaMP, has several side-effects. Here the authors show that GCaMP containing CaM interferes with gating and signaling of L-type calcium channels, which disrupts Ca 2+ dynamics and gene expression, and develop GCaMP-X to overcome these limitations.
GCaMP, one popular type of genetically-encoded Ca 2+ indicator, has been associated with various side-effects. Here we unveil the intrinsic problem prevailing over different versions and applications, showing that GCaMP containing CaM (calmodulin) interferes with both gating and signaling of L-type calcium channels (Ca V 1). GCaMP acts as an impaired apoCaM and Ca 2+ /CaM, both critical to Ca V 1, which disrupts Ca 2+ dynamics and gene expression. We then design and implement GCaMP-X, by incorporating an extra apoCaM-binding motif, effectively protecting Ca V 1-dependent excitation–transcription coupling from perturbations. GCaMP-X resolves the problems of detrimental nuclear accumulation, acute and chronic Ca 2+ dysregulation, and aberrant transcription signaling and cell morphogenesis, while still demonstrating excellent Ca 2+ -sensing characteristics partly inherited from GCaMP. In summary, CaM/Ca V 1 gating and signaling mechanisms are elucidated for GCaMP side-effects, while allowing the development of GCaMP-X to appropriately monitor cytosolic, submembrane or nuclear Ca 2+ , which is also expected to guide the future design of CaM-based molecular tools.
GCaMP, one popular type of genetically-encoded Ca2+ indicator, has been associated with various side-effects. Here we unveil the intrinsic problem prevailing over different versions and applications, showing that GCaMP containing CaM (calmodulin) interferes with both gating and signaling of L-type calcium channels (CaV1). GCaMP acts as an impaired apoCaM and Ca2+/CaM, both critical to CaV1, which disrupts Ca2+ dynamics and gene expression. We then design and implement GCaMP-X, by incorporating an extra apoCaM-binding motif, effectively protecting CaV1-dependent excitation–transcription coupling from perturbations. GCaMP-X resolves the problems of detrimental nuclear accumulation, acute and chronic Ca2+ dysregulation, and aberrant transcription signaling and cell morphogenesis, while still demonstrating excellent Ca2+-sensing characteristics partly inherited from GCaMP. In summary, CaM/CaV1 gating and signaling mechanisms are elucidated for GCaMP side-effects, while allowing the development of GCaMP-X to appropriately monitor cytosolic, submembrane or nuclear Ca2+, which is also expected to guide the future design of CaM-based molecular tools.
GCaMP, one popular type of genetically-encoded Ca2+ indicator, has been associated with various side-effects. Here we unveil the intrinsic problem prevailing over different versions and applications, showing that GCaMP containing CaM (calmodulin) interferes with both gating and signaling of L-type calcium channels (CaV1). GCaMP acts as an impaired apoCaM and Ca2+/CaM, both critical to CaV1, which disrupts Ca2+ dynamics and gene expression. We then design and implement GCaMP-X, by incorporating an extra apoCaM-binding motif, effectively protecting CaV1-dependent excitation–transcription coupling from perturbations. GCaMP-X resolves the problems of detrimental nuclear accumulation, acute and chronic Ca2+ dysregulation, and aberrant transcription signaling and cell morphogenesis, while still demonstrating excellent Ca2+-sensing characteristics partly inherited from GCaMP. In summary, CaM/CaV1 gating and signaling mechanisms are elucidated for GCaMP side-effects, while allowing the development of GCaMP-X to appropriately monitor cytosolic, submembrane or nuclear Ca2+, which is also expected to guide the future design of CaM-based molecular tools. The popular genetically-encoded Ca2+ indicator, GCaMP, has several side-effects. Here the authors show that GCaMP containing CaM interferes with gating and signaling of L-type calcium channels, which disrupts Ca2+ dynamics and gene expression, and develop GCaMP-X to overcome these limitations.
GCaMP, one popular type of genetically-encoded Ca2+ indicator, has been associated with various side-effects. Here we unveil the intrinsic problem prevailing over different versions and applications, showing that GCaMP containing CaM (calmodulin) interferes with both gating and signaling of L-type calcium channels (CaV1). GCaMP acts as an impaired apoCaM and Ca2+/CaM, both critical to CaV1, which disrupts Ca2+ dynamics and gene expression. We then design and implement GCaMP-X, by incorporating an extra apoCaM-binding motif, effectively protecting CaV1-dependent excitation-transcription coupling from perturbations. GCaMP-X resolves the problems of detrimental nuclear accumulation, acute and chronic Ca2+ dysregulation, and aberrant transcription signaling and cell morphogenesis, while still demonstrating excellent Ca2+-sensing characteristics partly inherited from GCaMP. In summary, CaM/CaV1 gating and signaling mechanisms are elucidated for GCaMP side-effects, while allowing the development of GCaMP-X to appropriately monitor cytosolic, submembrane or nuclear Ca2+, which is also expected to guide the future design of CaM-based molecular tools.GCaMP, one popular type of genetically-encoded Ca2+ indicator, has been associated with various side-effects. Here we unveil the intrinsic problem prevailing over different versions and applications, showing that GCaMP containing CaM (calmodulin) interferes with both gating and signaling of L-type calcium channels (CaV1). GCaMP acts as an impaired apoCaM and Ca2+/CaM, both critical to CaV1, which disrupts Ca2+ dynamics and gene expression. We then design and implement GCaMP-X, by incorporating an extra apoCaM-binding motif, effectively protecting CaV1-dependent excitation-transcription coupling from perturbations. GCaMP-X resolves the problems of detrimental nuclear accumulation, acute and chronic Ca2+ dysregulation, and aberrant transcription signaling and cell morphogenesis, while still demonstrating excellent Ca2+-sensing characteristics partly inherited from GCaMP. In summary, CaM/CaV1 gating and signaling mechanisms are elucidated for GCaMP side-effects, while allowing the development of GCaMP-X to appropriately monitor cytosolic, submembrane or nuclear Ca2+, which is also expected to guide the future design of CaM-based molecular tools.
The popular genetically-encoded Ca2+ indicator, GCaMP, has several side-effects. Here the authors show that GCaMP containing CaM interferes with gating and signaling of L-type calcium channels, which disrupts Ca2+ dynamics and gene expression, and develop GCaMP-X to overcome these limitations.
GCaMP, one popular type of genetically-encoded Ca indicator, has been associated with various side-effects. Here we unveil the intrinsic problem prevailing over different versions and applications, showing that GCaMP containing CaM (calmodulin) interferes with both gating and signaling of L-type calcium channels (Ca 1). GCaMP acts as an impaired apoCaM and Ca /CaM, both critical to Ca 1, which disrupts Ca dynamics and gene expression. We then design and implement GCaMP-X, by incorporating an extra apoCaM-binding motif, effectively protecting Ca 1-dependent excitation-transcription coupling from perturbations. GCaMP-X resolves the problems of detrimental nuclear accumulation, acute and chronic Ca dysregulation, and aberrant transcription signaling and cell morphogenesis, while still demonstrating excellent Ca -sensing characteristics partly inherited from GCaMP. In summary, CaM/Ca 1 gating and signaling mechanisms are elucidated for GCaMP side-effects, while allowing the development of GCaMP-X to appropriately monitor cytosolic, submembrane or nuclear Ca , which is also expected to guide the future design of CaM-based molecular tools.
ArticleNumber 1504
Author Ge, Lin
Zou, Linzhi
Liu, Xiaodong
Liu, Nan
Liu, Yuxia
Song, Sen
Yang, Yaxiong
He, Yuanyuan
Xiong, Wei
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  orcidid: 0000-0002-3313-6049
  surname: Yang
  fullname: Yang, Yaxiong
  organization: Department of Biomedical Engineering, School of Medicine, X-Lab for Transmembrane Signaling Research, Tsinghua University, School of Biological Science and Medical Engineering, Beihang University, Beijing Advanced Innovation Center for Biomedical Engineering, Beihang University, IDG/McGovern Institute for Brain Research, Tsinghua University
– sequence: 2
  givenname: Nan
  surname: Liu
  fullname: Liu, Nan
  organization: Department of Biomedical Engineering, School of Medicine, X-Lab for Transmembrane Signaling Research, Tsinghua University, School of Life Sciences, Yunan University
– sequence: 3
  givenname: Yuanyuan
  surname: He
  fullname: He, Yuanyuan
  organization: Department of Biomedical Engineering, School of Medicine, X-Lab for Transmembrane Signaling Research, Tsinghua University
– sequence: 4
  givenname: Yuxia
  surname: Liu
  fullname: Liu, Yuxia
  organization: Department of Biomedical Engineering, School of Medicine, X-Lab for Transmembrane Signaling Research, Tsinghua University
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  surname: Ge
  fullname: Ge, Lin
  organization: Department of Biomedical Engineering, School of Medicine, X-Lab for Transmembrane Signaling Research, Tsinghua University
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  givenname: Linzhi
  surname: Zou
  fullname: Zou, Linzhi
  organization: School of Life Sciences, Tsinghua University
– sequence: 7
  givenname: Sen
  surname: Song
  fullname: Song, Sen
  organization: Department of Biomedical Engineering, School of Medicine, X-Lab for Transmembrane Signaling Research, Tsinghua University, IDG/McGovern Institute for Brain Research, Tsinghua University
– sequence: 8
  givenname: Wei
  surname: Xiong
  fullname: Xiong, Wei
  organization: IDG/McGovern Institute for Brain Research, Tsinghua University, School of Life Sciences, Tsinghua University
– sequence: 9
  givenname: Xiaodong
  orcidid: 0000-0002-3171-9611
  surname: Liu
  fullname: Liu, Xiaodong
  email: liu-lab@vip.163.com
  organization: Department of Biomedical Engineering, School of Medicine, X-Lab for Transmembrane Signaling Research, Tsinghua University, School of Biological Science and Medical Engineering, Beihang University, Beijing Advanced Innovation Center for Biomedical Engineering, Beihang University, IDG/McGovern Institute for Brain Research, Tsinghua University, School of Life Sciences, Tsinghua University, Key Laboratory for Biomedical Engineering of Education Ministry, Zhejiang University
BackLink https://www.ncbi.nlm.nih.gov/pubmed/29666364$$D View this record in MEDLINE/PubMed
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Snippet GCaMP, one popular type of genetically-encoded Ca 2+ indicator, has been associated with various side-effects. Here we unveil the intrinsic problem prevailing...
GCaMP, one popular type of genetically-encoded Ca indicator, has been associated with various side-effects. Here we unveil the intrinsic problem prevailing...
GCaMP, one popular type of genetically-encoded Ca2+ indicator, has been associated with various side-effects. Here we unveil the intrinsic problem prevailing...
The popular genetically-encoded Ca2+ indicator, GCaMP, has several side-effects. Here the authors show that GCaMP containing CaM interferes with gating and...
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StartPage 1504
SubjectTerms 14/1
14/19
14/34
14/35
14/63
42/109
631/1647/245/2225
631/378/2586
631/45/269/1146
631/80/86/1999
631/80/86/2372
9/10
9/74
96/95
Animals
Biosensing Techniques - methods
Calcium - chemistry
Calcium - metabolism
Calcium channels
Calcium channels (L-type)
Calcium channels (voltage-gated)
Calcium Channels, L-Type - metabolism
Calcium imaging
Calcium ions
Calcium Signaling
Calcium signalling
Calcium-binding protein
Calmodulin
Calmodulin - chemistry
Calmodulin - genetics
Calmodulin - metabolism
Channel gating
Coupling (molecular)
Fluorescent Dyes - chemistry
Gene expression
Genetic Engineering - methods
Green Fluorescent Proteins - chemistry
Green Fluorescent Proteins - genetics
HEK293 Cells
Humanities and Social Sciences
Humans
Intravital Microscopy - methods
Ion Channel Gating
Mice
Mice, Inbred ICR
Molecular Imaging - methods
Morphogenesis
multidisciplinary
Neurons
Patch-Clamp Techniques
Primary Cell Culture
Protein Binding
Science
Science (multidisciplinary)
Side effects
Transcription
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Title Improved calcium sensor GCaMP-X overcomes the calcium channel perturbations induced by the calmodulin in GCaMP
URI https://link.springer.com/article/10.1038/s41467-018-03719-6
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