Dynamics of the association of heat shock protein HSPA6 (Hsp70B’) and HSPA1A (Hsp70–1) with stress-sensitive cytoplasmic and nuclear structures in differentiated human neuronal cells
Identifieur interne : 000214 ( Pmc/Corpus ); précédent : 000213; suivant : 000215Dynamics of the association of heat shock protein HSPA6 (Hsp70B’) and HSPA1A (Hsp70–1) with stress-sensitive cytoplasmic and nuclear structures in differentiated human neuronal cells
Auteurs : Sadek Shorbagi ; Ian R. BrownSource :
- Cell Stress & Chaperones [ 1355-8145 ] ; 2016.
Abstract
Heat shock proteins (Hsps) are cellular repair agents that counter the effects of protein misfolding that is a characteristic feature of neurodegenerative diseases. HSPA1A (Hsp70–1) is a widely studied member of the HSPA (Hsp70) family. The little-studied HSPA6 (Hsp70B’) is present in the human genome and absent in mouse and rat; hence, it is missing in current animal models of neurodegenerative diseases. Differentiated human neuronal SH-SY5Y cells were employed to compare the dynamics of the association of YFP-tagged HSPA6 and HSPA1A with stress-sensitive cytoplasmic and nuclear structures. Following thermal stress, live-imaging confocal microscopy and
The online version of this article (doi:10.1007/s12192-016-0724-2) contains supplementary material, which is available to authorized users.
Url:
DOI: 10.1007/s12192-016-0724-2
PubMed: 27527722
PubMed Central: 5083669
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PMC:5083669Le document en format XML
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<author><name sortKey="Shorbagi, Sadek" sort="Shorbagi, Sadek" uniqKey="Shorbagi S" first="Sadek" last="Shorbagi">Sadek Shorbagi</name>
<affiliation><nlm:aff id="Aff1">Centre for the Neurobiology of Stress, Department of Biological Sciences, University of Toronto Scarborough, Toronto, ON M1C 1A4 Canada</nlm:aff>
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<author><name sortKey="Brown, Ian R" sort="Brown, Ian R" uniqKey="Brown I" first="Ian R." last="Brown">Ian R. Brown</name>
<affiliation><nlm:aff id="Aff1">Centre for the Neurobiology of Stress, Department of Biological Sciences, University of Toronto Scarborough, Toronto, ON M1C 1A4 Canada</nlm:aff>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Dynamics of the association of heat shock protein HSPA6 (Hsp70B’) and HSPA1A (Hsp70–1) with stress-sensitive cytoplasmic and nuclear structures in differentiated human neuronal cells</title>
<author><name sortKey="Shorbagi, Sadek" sort="Shorbagi, Sadek" uniqKey="Shorbagi S" first="Sadek" last="Shorbagi">Sadek Shorbagi</name>
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<author><name sortKey="Brown, Ian R" sort="Brown, Ian R" uniqKey="Brown I" first="Ian R." last="Brown">Ian R. Brown</name>
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<series><title level="j">Cell Stress & Chaperones</title>
<idno type="ISSN">1355-8145</idno>
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<front><div type="abstract" xml:lang="en"><p>Heat shock proteins (Hsps) are cellular repair agents that counter the effects of protein misfolding that is a characteristic feature of neurodegenerative diseases. HSPA1A (Hsp70–1) is a widely studied member of the HSPA (Hsp70) family. The little-studied HSPA6 (Hsp70B’) is present in the human genome and absent in mouse and rat; hence, it is missing in current animal models of neurodegenerative diseases. Differentiated human neuronal SH-SY5Y cells were employed to compare the dynamics of the association of YFP-tagged HSPA6 and HSPA1A with stress-sensitive cytoplasmic and nuclear structures. Following thermal stress, live-imaging confocal microscopy and <italic>F</italic>
luorescence <italic>R</italic>
ecovery <italic>A</italic>
fter <italic>P</italic>
hotobleaching (FRAP) demonstrated that HSPA6 displayed a prolonged and more dynamic association, compared to HSPA1A, with centrioles that play critical roles in neuronal polarity and migration. HSPA6 and HSPA1A also targeted nuclear speckles, rich in RNA splicing factors, and the granular component of the nucleolus that is involved in rRNA processing and ribosomal subunit assembly. HSPA6 and HSPA1A displayed similar FRAP kinetics in their interaction with nuclear speckles and the nucleolus. Subsequently, during the recovery from neuronal stress, HSPA6, but not HSPA1A, localized with the periphery of nuclear speckles (perispeckles) that have been characterized as transcription sites. The stress-induced association of HSPA6 with perispeckles displayed the greatest dynamism compared to the interaction of HSPA6 or HSPA1A with other stress-sensitive cytoplasmic and nuclear structures. This suggests involvement of HSPA6 in transcriptional recovery of human neurons from cellular stress that is not apparent for HSPA1A.</p>
<sec><title>Electronic supplementary material</title>
<p>The online version of this article (doi:10.1007/s12192-016-0724-2) contains supplementary material, which is available to authorized users.</p>
</sec>
</div>
</front>
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<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Cell Stress Chaperones</journal-id>
<journal-id journal-id-type="iso-abbrev">Cell Stress Chaperones</journal-id>
<journal-title-group><journal-title>Cell Stress & Chaperones</journal-title>
</journal-title-group>
<issn pub-type="ppub">1355-8145</issn>
<issn pub-type="epub">1466-1268</issn>
<publisher><publisher-name>Springer Netherlands</publisher-name>
<publisher-loc>Dordrecht</publisher-loc>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">27527722</article-id>
<article-id pub-id-type="pmc">5083669</article-id>
<article-id pub-id-type="publisher-id">724</article-id>
<article-id pub-id-type="doi">10.1007/s12192-016-0724-2</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Original Paper</subject>
</subj-group>
</article-categories>
<title-group><article-title>Dynamics of the association of heat shock protein HSPA6 (Hsp70B’) and HSPA1A (Hsp70–1) with stress-sensitive cytoplasmic and nuclear structures in differentiated human neuronal cells</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Shorbagi</surname>
<given-names>Sadek</given-names>
</name>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<contrib contrib-type="author" corresp="yes"><name><surname>Brown</surname>
<given-names>Ian R.</given-names>
</name>
<address><phone>(416) 287-7413</phone>
<email>ibrown@utsc.utoronto.ca</email>
</address>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<aff id="Aff1">Centre for the Neurobiology of Stress, Department of Biological Sciences, University of Toronto Scarborough, Toronto, ON M1C 1A4 Canada</aff>
</contrib-group>
<pub-date pub-type="epub"><day>16</day>
<month>8</month>
<year>2016</year>
</pub-date>
<pub-date pub-type="ppub"><month>11</month>
<year>2016</year>
</pub-date>
<volume>21</volume>
<issue>6</issue>
<fpage>993</fpage>
<lpage>1003</lpage>
<history><date date-type="received"><day>13</day>
<month>6</month>
<year>2016</year>
</date>
<date date-type="rev-recd"><day>11</day>
<month>7</month>
<year>2016</year>
</date>
<date date-type="accepted"><day>17</day>
<month>7</month>
<year>2016</year>
</date>
</history>
<permissions><copyright-statement>© Cell Stress Society International 2016</copyright-statement>
</permissions>
<abstract id="Abs1"><p>Heat shock proteins (Hsps) are cellular repair agents that counter the effects of protein misfolding that is a characteristic feature of neurodegenerative diseases. HSPA1A (Hsp70–1) is a widely studied member of the HSPA (Hsp70) family. The little-studied HSPA6 (Hsp70B’) is present in the human genome and absent in mouse and rat; hence, it is missing in current animal models of neurodegenerative diseases. Differentiated human neuronal SH-SY5Y cells were employed to compare the dynamics of the association of YFP-tagged HSPA6 and HSPA1A with stress-sensitive cytoplasmic and nuclear structures. Following thermal stress, live-imaging confocal microscopy and <italic>F</italic>
luorescence <italic>R</italic>
ecovery <italic>A</italic>
fter <italic>P</italic>
hotobleaching (FRAP) demonstrated that HSPA6 displayed a prolonged and more dynamic association, compared to HSPA1A, with centrioles that play critical roles in neuronal polarity and migration. HSPA6 and HSPA1A also targeted nuclear speckles, rich in RNA splicing factors, and the granular component of the nucleolus that is involved in rRNA processing and ribosomal subunit assembly. HSPA6 and HSPA1A displayed similar FRAP kinetics in their interaction with nuclear speckles and the nucleolus. Subsequently, during the recovery from neuronal stress, HSPA6, but not HSPA1A, localized with the periphery of nuclear speckles (perispeckles) that have been characterized as transcription sites. The stress-induced association of HSPA6 with perispeckles displayed the greatest dynamism compared to the interaction of HSPA6 or HSPA1A with other stress-sensitive cytoplasmic and nuclear structures. This suggests involvement of HSPA6 in transcriptional recovery of human neurons from cellular stress that is not apparent for HSPA1A.</p>
<sec><title>Electronic supplementary material</title>
<p>The online version of this article (doi:10.1007/s12192-016-0724-2) contains supplementary material, which is available to authorized users.</p>
</sec>
</abstract>
<kwd-group xml:lang="en"><title>Keywords</title>
<kwd>HSPA6 (Hsp70B’)</kwd>
<kwd>HSPA1A (Hsp70–1)</kwd>
<kwd>FRAP</kwd>
<kwd>Live imaging</kwd>
<kwd>SH-SY5Y</kwd>
</kwd-group>
<funding-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/501100000038</institution-id>
<institution>Natural Sciences and Engineering Research Council of Canada</institution>
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</funding-source>
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<custom-meta-group><custom-meta><meta-name>issue-copyright-statement</meta-name>
<meta-value>© Cell Stress Society International 2016</meta-value>
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