Redox regulation of cytoskeletal dynamics during differentiation and de-differentiation.
Identifieur interne : 000512 ( Main/Exploration ); précédent : 000511; suivant : 000513Redox regulation of cytoskeletal dynamics during differentiation and de-differentiation.
Auteurs : Manuela Gellert [Allemagne] ; Eva-Maria Hanschmann [Allemagne] ; Klaudia Lepka [Allemagne] ; Carsten Berndt [Allemagne] ; Christopher Horst Lillig [Allemagne]Source :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2015.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Cytosquelette (métabolisme), Différenciation cellulaire (physiologie), Dédifférenciation cellulaire (physiologie), Humains (MeSH), Maladies neurodégénératives (métabolisme), Maladies neurodégénératives (physiopathologie), Modèles biologiques (MeSH), Oxydoréduction (MeSH), Protéines du cytosquelette (métabolisme), Tumeurs (métabolisme), Tumeurs (physiopathologie).
- MESH :
- métabolisme : Cytosquelette, Maladies neurodégénératives, Protéines du cytosquelette, Tumeurs.
- physiologie : Différenciation cellulaire, Dédifférenciation cellulaire.
- physiopathologie : Maladies neurodégénératives, Tumeurs.
- Animaux, Humains, Modèles biologiques, Oxydoréduction.
English descriptors
- KwdEn :
- Animals (MeSH), Cell Dedifferentiation (physiology), Cell Differentiation (physiology), Cytoskeletal Proteins (metabolism), Cytoskeleton (metabolism), Humans (MeSH), Models, Biological (MeSH), Neoplasms (metabolism), Neoplasms (physiopathology), Neurodegenerative Diseases (metabolism), Neurodegenerative Diseases (physiopathology), Oxidation-Reduction (MeSH).
- MESH :
- chemical , metabolism : Cytoskeletal Proteins.
- metabolism : Cytoskeleton, Neoplasms, Neurodegenerative Diseases.
- physiology : Cell Dedifferentiation, Cell Differentiation.
- physiopathology : Neoplasms, Neurodegenerative Diseases.
- Animals, Humans, Models, Biological, Oxidation-Reduction.
Abstract
BACKGROUND
The cytoskeleton, unlike the bony vertebrate skeleton or the exoskeleton of invertebrates, is a highly dynamic meshwork of protein filaments that spans through the cytosol of eukaryotic cells. Especially actin filaments and microtubuli do not only provide structure and points of attachments, but they also shape cells, they are the basis for intracellular transport and distribution, all types of cell movement, and--through specific junctions and points of adhesion--join cells together to form tissues, organs, and organisms.
SCOPE OF REVIEW
The fine tuned regulation of cytoskeletal dynamics is thus indispensible for cell differentiation and all developmental processes. Here, we discussed redox signalling mechanisms that control this dynamic remodeling. Foremost, we emphasised recent discoveries that demonstrated reversible thiol and methionyl switches in the regulation of actin dynamics.
MAJOR CONCLUSIONS
Thiol and methionyl switches play an essential role in the regulation of cytoskeletal dynamics.
GENERAL SIGNIFICANCE
The dynamic remodeling of the cytoskeleton is controlled by various redox switches. These mechanisms are indispensible during development and organogenesis and might contribute to numerous pathological conditions. This article is part of a Special Issue entitled Redox regulation of differentiation and de-differentiation.
DOI: 10.1016/j.bbagen.2014.10.030
PubMed: 25450486
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Especially actin filaments and microtubuli do not only provide structure and points of attachments, but they also shape cells, they are the basis for intracellular transport and distribution, all types of cell movement, and--through specific junctions and points of adhesion--join cells together to form tissues, organs, and organisms.</p></div><div type="abstract" xml:lang="en"><p><b>SCOPE OF REVIEW</b></p><p>The fine tuned regulation of cytoskeletal dynamics is thus indispensible for cell differentiation and all developmental processes. Here, we discussed redox signalling mechanisms that control this dynamic remodeling. Foremost, we emphasised recent discoveries that demonstrated reversible thiol and methionyl switches in the regulation of actin dynamics.</p></div><div type="abstract" xml:lang="en"><p><b>MAJOR CONCLUSIONS</b></p><p>Thiol and methionyl switches play an essential role in the regulation of cytoskeletal dynamics.</p></div><div type="abstract" xml:lang="en"><p><b>GENERAL SIGNIFICANCE</b></p><p>The dynamic remodeling of the cytoskeleton is controlled by various redox switches. These mechanisms are indispensible during development and organogenesis and might contribute to numerous pathological conditions. This article is part of a Special Issue entitled Redox regulation of differentiation and de-differentiation.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25450486</PMID><DateCompleted><Year>2015</Year><Month>09</Month><Day>30</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1850</Volume><Issue>8</Issue><PubDate><Year>2015</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Redox regulation of cytoskeletal dynamics during differentiation and de-differentiation.</ArticleTitle><Pagination><MedlinePgn>1575-87</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbagen.2014.10.030</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0304-4165(14)00367-5</ELocationID><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">The cytoskeleton, unlike the bony vertebrate skeleton or the exoskeleton of invertebrates, is a highly dynamic meshwork of protein filaments that spans through the cytosol of eukaryotic cells. Especially actin filaments and microtubuli do not only provide structure and points of attachments, but they also shape cells, they are the basis for intracellular transport and distribution, all types of cell movement, and--through specific junctions and points of adhesion--join cells together to form tissues, organs, and organisms.</AbstractText><AbstractText Label="SCOPE OF REVIEW" NlmCategory="METHODS">The fine tuned regulation of cytoskeletal dynamics is thus indispensible for cell differentiation and all developmental processes. Here, we discussed redox signalling mechanisms that control this dynamic remodeling. Foremost, we emphasised recent discoveries that demonstrated reversible thiol and methionyl switches in the regulation of actin dynamics.</AbstractText><AbstractText Label="MAJOR CONCLUSIONS" NlmCategory="CONCLUSIONS">Thiol and methionyl switches play an essential role in the regulation of cytoskeletal dynamics.</AbstractText><AbstractText Label="GENERAL SIGNIFICANCE" NlmCategory="CONCLUSIONS">The dynamic remodeling of the cytoskeleton is controlled by various redox switches. These mechanisms are indispensible during development and organogenesis and might contribute to numerous pathological conditions. This article is part of a Special Issue entitled Redox regulation of differentiation and de-differentiation.</AbstractText><CopyrightInformation>Copyright © 2014 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gellert</LastName><ForeName>Manuela</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institut für Biochemie und Molekularbiologie, Universitätsmedizin Greifswald, Ernst-Moritz-Arndt-Universität, Greifswald, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hanschmann</LastName><ForeName>Eva-Maria</ForeName><Initials>EM</Initials><AffiliationInfo><Affiliation>Institut für Biochemie und Molekularbiologie, Universitätsmedizin Greifswald, Ernst-Moritz-Arndt-Universität, Greifswald, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lepka</LastName><ForeName>Klaudia</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Klinik für Neurologie, Medizinische Fakultät, Heinrich-Heine-Universität, Düsseldorf, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Berndt</LastName><ForeName>Carsten</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Klinik für Neurologie, Medizinische Fakultät, Heinrich-Heine-Universität, Düsseldorf, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lillig</LastName><ForeName>Christopher Horst</ForeName><Initials>CH</Initials><AffiliationInfo><Affiliation>Institut für Biochemie und Molekularbiologie, Universitätsmedizin Greifswald, Ernst-Moritz-Arndt-Universität, Greifswald, Germany. Electronic address: horst@lillig.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>11</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003598">Cytoskeletal Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054337" MajorTopicYN="N">Cell Dedifferentiation</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002454" MajorTopicYN="N">Cell Differentiation</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003598" MajorTopicYN="N">Cytoskeletal Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003599" MajorTopicYN="N">Cytoskeleton</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009369" MajorTopicYN="N">Neoplasms</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000503" MajorTopicYN="N">physiopathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019636" MajorTopicYN="N">Neurodegenerative Diseases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000503" MajorTopicYN="N">physiopathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Cytoskeleton remodeling</Keyword><Keyword MajorTopicYN="N">Glutaredoxin</Keyword><Keyword MajorTopicYN="N">Methionine sulfoxide reductase</Keyword><Keyword MajorTopicYN="N">Redox signaling</Keyword><Keyword MajorTopicYN="N">Redox switch</Keyword><Keyword MajorTopicYN="N">Thioredoxin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>09</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>10</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>10</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>12</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>12</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>10</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25450486</ArticleId><ArticleId IdType="pii">S0304-4165(14)00367-5</ArticleId><ArticleId IdType="doi">10.1016/j.bbagen.2014.10.030</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>District de Düsseldorf</li><li>Rhénanie-du-Nord-Westphalie</li></region><settlement><li>Düsseldorf</li></settlement></list><tree><country name="Allemagne"><noRegion><name sortKey="Gellert, Manuela" sort="Gellert, Manuela" uniqKey="Gellert M" first="Manuela" last="Gellert">Manuela Gellert</name></noRegion><name sortKey="Berndt, Carsten" sort="Berndt, Carsten" uniqKey="Berndt C" first="Carsten" last="Berndt">Carsten Berndt</name><name sortKey="Hanschmann, Eva Maria" sort="Hanschmann, Eva Maria" uniqKey="Hanschmann E" first="Eva-Maria" last="Hanschmann">Eva-Maria Hanschmann</name><name sortKey="Lepka, Klaudia" sort="Lepka, Klaudia" uniqKey="Lepka K" first="Klaudia" last="Lepka">Klaudia Lepka</name><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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