PFA fixation enables artifact-free super-resolution imaging of the actin cytoskeleton and associated proteins

Super-resolution microscopy (SRM) allows precise localization of proteins in cellular organelles and structures, including the actin cytoskeleton. Yet sample preparation protocols for SRM are rather anecdotal and still being optimized. Thus, SRM-based imaging of the actin cytoskeleton and associated...

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Veröffentlicht in:Biology open Jg. 5; H. 7; S. 1001 - 1009
Hauptverfasser: Leyton-Puig, Daniela, Kedziora, Katarzyna M., Isogai, Tadamoto, van den Broek, Bram, Jalink, Kees, Innocenti, Metello
Format: Journal Article
Sprache:Englisch
Veröffentlicht: England The Company of Biologists Ltd 15.07.2016
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ISSN:2046-6390, 2046-6390
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Abstract Super-resolution microscopy (SRM) allows precise localization of proteins in cellular organelles and structures, including the actin cytoskeleton. Yet sample preparation protocols for SRM are rather anecdotal and still being optimized. Thus, SRM-based imaging of the actin cytoskeleton and associated proteins often remains challenging and poorly reproducible. Here, we show that proper paraformaldehyde (PFA)-based sample preparation preserves the architecture of the actin cytoskeleton almost as faithfully as gold-standard glutaraldehyde fixation. We show that this fixation is essential for proper immuno-based localization of actin-binding and actin-regulatory proteins involved in the formation of lamellipodia and ruffles, such as mDia1, WAVE2 and clathrin heavy chain, and provide detailed guidelines for the execution of our method. In summary, proper PFA-based sample preparation increases the multi-color possibilities and the reproducibility of SRM of the actin cytoskeleton and its associated proteins.
AbstractList Super-resolution microscopy (SRM) allows precise localization of proteins in cellular organelles and structures, including the actin cytoskeleton. Yet sample preparation protocols for SRM are rather anecdotal and still being optimized. Thus, SRM-based imaging of the actin cytoskeleton and associated proteins often remains challenging and poorly reproducible. Here, we show that proper paraformaldehyde (PFA)-based sample preparation preserves the architecture of the actin cytoskeleton almost as faithfully as gold-standard glutaraldehyde fixation. We show that this fixation is essential for proper immuno-based localization of actin-binding and actin-regulatory proteins involved in the formation of lamellipodia and ruffles, such as mDia1, WAVE2 and clathrin heavy chain, and provide detailed guidelines for the execution of our method. In summary, proper PFA-based sample preparation increases the multi-color possibilities and the reproducibility of SRM of the actin cytoskeleton and its associated proteins.Super-resolution microscopy (SRM) allows precise localization of proteins in cellular organelles and structures, including the actin cytoskeleton. Yet sample preparation protocols for SRM are rather anecdotal and still being optimized. Thus, SRM-based imaging of the actin cytoskeleton and associated proteins often remains challenging and poorly reproducible. Here, we show that proper paraformaldehyde (PFA)-based sample preparation preserves the architecture of the actin cytoskeleton almost as faithfully as gold-standard glutaraldehyde fixation. We show that this fixation is essential for proper immuno-based localization of actin-binding and actin-regulatory proteins involved in the formation of lamellipodia and ruffles, such as mDia1, WAVE2 and clathrin heavy chain, and provide detailed guidelines for the execution of our method. In summary, proper PFA-based sample preparation increases the multi-color possibilities and the reproducibility of SRM of the actin cytoskeleton and its associated proteins.
Super-resolution microscopy (SRM) allows precise localization of proteins in cellular organelles and structures, including the actin cytoskeleton. Yet sample preparation protocols for SRM are rather anecdotal and still being optimized. Thus, SRM-based imaging of the actin cytoskeleton and associated proteins often remains challenging and poorly reproducible. Here, we show that proper paraformaldehyde (PFA)-based sample preparation preserves the architecture of the actin cytoskeleton almost as faithfully as gold-standard glutaraldehyde fixation. We show that this fixation is essential for proper immuno-based localization of actin-binding and actin-regulatory proteins involved in the formation of lamellipodia and ruffles, such as mDia1, WAVE2 and clathrin heavy chain, and provide detailed guidelines for the execution of our method. In summary, proper PFA-based sample preparation increases the multi-color possibilities and the reproducibility of SRM of the actin cytoskeleton and its associated proteins. Summary: We show that proper PFA fixation allows high-quality super-resolution imaging of the actin cytoskeleton and can outperform gold-standard glutaraldehyde fixation for imaging of actin-binding proteins.
Super-resolution microscopy (SRM) allows precise localization of proteins in cellular organelles and structures, including the actin cytoskeleton. Yet sample preparation protocols for SRM are rather anecdotal and still being optimized. Thus, SRM-based imaging of the actin cytoskeleton and associated proteins often remains challenging and poorly reproducible. Here, we show that proper paraformaldehyde (PFA)-based sample preparation preserves the architecture of the actin cytoskeleton almost as faithfully as gold-standard glutaraldehyde fixation. We show that this fixation is essential for proper immuno-based localization of actin-binding and actin-regulatory proteins involved in the formation of lamellipodia and ruffles, such as mDia1, WAVE2 and clathrin heavy chain, and provide detailed guidelines for the execution of our method. In summary, proper PFA-based sample preparation increases the multi-color possibilities and the reproducibility of SRM of the actin cytoskeleton and its associated proteins.
Author Innocenti, Metello
Kedziora, Katarzyna M.
Jalink, Kees
van den Broek, Bram
Isogai, Tadamoto
Leyton-Puig, Daniela
AuthorAffiliation 1 Division of Cell Biology I , The Netherlands Cancer Institute , Plesmanlaan 121, Amsterdam 1066 CX , The Netherlands
2 Division of Molecular Genetics , The Netherlands Cancer Institute , Plesmanlaan 121, Amsterdam 1066 CX , The Netherlands
AuthorAffiliation_xml – name: 2 Division of Molecular Genetics , The Netherlands Cancer Institute , Plesmanlaan 121, Amsterdam 1066 CX , The Netherlands
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  givenname: Daniela
  surname: Leyton-Puig
  fullname: Leyton-Puig, Daniela
  organization: Division of Cell Biology I, The Netherlands Cancer Institute, Plesmanlaan 121, Amsterdam 1066 CX, The Netherlands
– sequence: 2
  givenname: Katarzyna M.
  surname: Kedziora
  fullname: Kedziora, Katarzyna M.
  organization: Division of Cell Biology I, The Netherlands Cancer Institute, Plesmanlaan 121, Amsterdam 1066 CX, The Netherlands
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  givenname: Tadamoto
  surname: Isogai
  fullname: Isogai, Tadamoto
  organization: Division of Molecular Genetics, The Netherlands Cancer Institute, Plesmanlaan 121, Amsterdam 1066 CX, The Netherlands
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  givenname: Bram
  surname: van den Broek
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  givenname: Metello
  orcidid: 0000-0002-7455-2559
  surname: Innocenti
  fullname: Innocenti, Metello
  organization: Division of Molecular Genetics, The Netherlands Cancer Institute, Plesmanlaan 121, Amsterdam 1066 CX, The Netherlands
BackLink https://www.ncbi.nlm.nih.gov/pubmed/27378434$$D View this record in MEDLINE/PubMed
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Keywords Protein localization
dSTORM
Fixation
Actin cytoskeleton
Super-resolution microscopy (SRM)
Language English
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SubjectTerms Actin
Actin cytoskeleton
Cellular structure
Clathrin
Cytoskeleton
dSTORM
Fixation
Image resolution
Lamellipodia
Localization
Methods & Techniques
Organelles
Protein localization
Proteins
Pseudopodia
Regulatory proteins
Reproducibility
Sample preparation
Super-resolution microscopy (SRM)
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Title PFA fixation enables artifact-free super-resolution imaging of the actin cytoskeleton and associated proteins
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