CDC25B associates with a centrin 2‐containing complex and is involved in maintaining centrosome integrity
Identifieur interne : 001936 ( Istex/Corpus ); précédent : 001935; suivant : 001937CDC25B associates with a centrin 2‐containing complex and is involved in maintaining centrosome integrity
Auteurs : Rose Boutros ; Corinne Lorenzo ; Odile Mondesert ; Alain Jauneau ; Vanessa Oakes ; Christine Dozier ; Brian Gabrielli ; Bernard DucommunSource :
- Biology of the Cell [ 0248-4900 ] ; 2011-02.
English descriptors
- KwdEn :
- Association figure, Authors journal compilation, Biol, Bornens, Boutros, Brian gabrielli, Catalytic activity, Cell biol, Cell cycle, Cell division cycle, Centrin, Centriole, Centriole assembly, Centriole biogenesis, Centriole duplication, Centrosomal, Centrosomal ctn2, Centrosomal levels, Centrosomal localization, Centrosomal pool, Centrosome, Centrosome duplication, Centrosome integrity, Centrosome levels, Chk1, Christine dozier, Corinne lorenzo, Ctn1, Ctn2, Ctn2 sirna duplexes, Ctn3, Ctns, Curie institute, Ducommun, Duplex, Endogenous, Endogenous ctn2, Flim, Fusion proteins, Gabrielli, Hela, Hela cells, Human cells, Human centrin, Imaging, Independent experiments, Localization, Lysis buffer, Mammalian cells, Michel bornens, Microtubule, Morange, Mother centriole, Multiple centrosome proteins, Mutant, Nitrocellulose membranes, Nucleotide excision repair, Odile mondesert, Others figure, Overall integrity, Phosphatase, Portland press, Present study, Protease inhibitors, Protein complexes, Protein extracts, Research article, Santa cruz biotechnology, Sirna, Sirna duplexes, Streak camera, Supplementary figure, Toulouse, Tubulin, U2os, U2os cells, Uorescence, Uorescence lifetime, Uorescence lifetime imaging microscopy, Xeroderma pigmentosum group.
- Teeft :
- Association figure, Authors journal compilation, Biol, Bornens, Boutros, Brian gabrielli, Catalytic activity, Cell biol, Cell cycle, Cell division cycle, Centrin, Centriole, Centriole assembly, Centriole biogenesis, Centriole duplication, Centrosomal, Centrosomal ctn2, Centrosomal levels, Centrosomal localization, Centrosomal pool, Centrosome, Centrosome duplication, Centrosome integrity, Centrosome levels, Chk1, Christine dozier, Corinne lorenzo, Ctn1, Ctn2, Ctn2 sirna duplexes, Ctn3, Ctns, Curie institute, Ducommun, Duplex, Endogenous, Endogenous ctn2, Flim, Fusion proteins, Gabrielli, Hela, Hela cells, Human cells, Human centrin, Imaging, Independent experiments, Localization, Lysis buffer, Mammalian cells, Michel bornens, Microtubule, Morange, Mother centriole, Multiple centrosome proteins, Mutant, Nitrocellulose membranes, Nucleotide excision repair, Odile mondesert, Others figure, Overall integrity, Phosphatase, Portland press, Present study, Protease inhibitors, Protein complexes, Protein extracts, Research article, Santa cruz biotechnology, Sirna, Sirna duplexes, Streak camera, Supplementary figure, Toulouse, Tubulin, U2os, U2os cells, Uorescence, Uorescence lifetime, Uorescence lifetime imaging microscopy, Xeroderma pigmentosum group.
Abstract
Background information. CDC25 (cell division cycle 25) phosphatases function as activators of CDK (cyclin‐dependent kinase)–cyclin complexes to regulate progression through the CDC. We have recently identified a pool of CDC25B at the centrosome of interphase cells that plays a role in regulating centrosome numbers. Results. In the present study, we demonstrate that CDC25B forms a close association with Ctn (centrin) proteins at the centrosome. This interaction involves both N‐ and C‐terminal regions of CDC25B and requires CDC25B binding to its CDK—cyclin substrates. However, the interaction is not dependent on the enzyme activity of CDC25B. Although CDC25B appears to bind indirectly to Ctn2, this association is pertinent to CDC25B localization at the centrosome. We further demonstrate that CDC25B plays a role in maintaining the overall integrity of the centrosome, by regulating the centrosome levels of multiple centrosome proteins, including that of Ctn2. Conclusions. Our results therefore suggest that CDC25B associates with a Ctn2‐containing multiprotein complex in the cytoplasm, which targets it to the centrosome, where it plays a role in maintaining the centrosome levels of Ctn2 and a number of other centrosome components.
Url:
DOI: 10.1042/BC20100111
Links to Exploration step
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<front><div type="abstract" xml:lang="en">Background information. CDC25 (cell division cycle 25) phosphatases function as activators of CDK (cyclin‐dependent kinase)–cyclin complexes to regulate progression through the CDC. We have recently identified a pool of CDC25B at the centrosome of interphase cells that plays a role in regulating centrosome numbers. Results. In the present study, we demonstrate that CDC25B forms a close association with Ctn (centrin) proteins at the centrosome. This interaction involves both N‐ and C‐terminal regions of CDC25B and requires CDC25B binding to its CDK—cyclin substrates. However, the interaction is not dependent on the enzyme activity of CDC25B. Although CDC25B appears to bind indirectly to Ctn2, this association is pertinent to CDC25B localization at the centrosome. We further demonstrate that CDC25B plays a role in maintaining the overall integrity of the centrosome, by regulating the centrosome levels of multiple centrosome proteins, including that of Ctn2. Conclusions. Our results therefore suggest that CDC25B associates with a Ctn2‐containing multiprotein complex in the cytoplasm, which targets it to the centrosome, where it plays a role in maintaining the centrosome levels of Ctn2 and a number of other centrosome components.</div>
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. CDC25 (cell division cycle 25) phosphatases function as activators of CDK (cyclin‐dependent kinase)–cyclin complexes to regulate progression through the CDC. We have recently identified a pool of CDC25B at the centrosome of interphase cells that plays a role in regulating centrosome numbers.</p>
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. In the present study, we demonstrate that CDC25B forms a close association with Ctn (centrin) proteins at the centrosome. This interaction involves both N‐ and C‐terminal regions of CDC25B and requires CDC25B binding to its CDK—cyclin substrates. However, the interaction is not dependent on the enzyme activity of CDC25B. Although CDC25B appears to bind indirectly to Ctn2, this association is pertinent to CDC25B localization at the centrosome. We further demonstrate that CDC25B plays a role in maintaining the overall integrity of the centrosome, by regulating the centrosome levels of multiple centrosome proteins, including that of Ctn2.</p>
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. Our results therefore suggest that CDC25B associates with a Ctn2‐containing multiprotein complex in the cytoplasm, which targets it to the centrosome, where it plays a role in maintaining the centrosome levels of Ctn2 and a number of other centrosome components.</p>
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<creator creatorRole="author" xml:id="cr6" affiliationRef="#a2 #a3"><personName><givenNames>Christine</givenNames>
<familyName>Dozier</familyName>
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<creator creatorRole="author" xml:id="cr7" affiliationRef="#a1"><personName><givenNames>Brian</givenNames>
<familyName>Gabrielli</familyName>
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<creator creatorRole="author" xml:id="cr8" affiliationRef="#a2 #a3 #a5" corresponding="yes"><personName><givenNames>Bernard</givenNames>
<familyName>Ducommun</familyName>
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<affiliationGroup><affiliation xml:id="a1" countryCode="AU"><unparsedAffiliation>Diamantina Institute, Princess Alexandra Hospital, The University of Queensland, Brisbane, Australia</unparsedAffiliation>
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<affiliation xml:id="a2" countryCode="FR"><unparsedAffiliation>Université de Toulouse, LBCMCP, 118 route de Narbonne, F‐31062 Toulouse, France</unparsedAffiliation>
</affiliation>
<affiliation xml:id="a3" countryCode="FR"><unparsedAffiliation>Centre National de la Recherche Scientifique (CNRS), LBCMCP‐UMR5088, F‐31062 Toulouse, France</unparsedAffiliation>
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<affiliation xml:id="a4" countryCode="FR"><unparsedAffiliation>CNRS, Plateforme Imagerie, Pôle de Biotechnologie Végétale, F‐31320 Castanet Tolosan, France</unparsedAffiliation>
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<affiliation xml:id="a5" countryCode="FR"><unparsedAffiliation>CHU Purpan, Service d'Hématologie, TSA 40031, F‐31059 Toulouse, France</unparsedAffiliation>
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<keywordGroup xml:lang="en"><keyword xml:id="k1">CDC25B</keyword>
<keyword xml:id="k2">centrin (Ctn)</keyword>
<keyword xml:id="k3">centrosome</keyword>
<keyword xml:id="k4">cyclin‐dependent kinase (CDK)</keyword>
<keyword xml:id="k5">fluorescence lifetime imaging microscopy (FLIM)</keyword>
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<supportingInformation><p>Supporting Information</p>
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<abstractGroup><abstract type="main" xml:lang="en"><p><i>Background information</i>
. CDC25 (cell division cycle 25) phosphatases function as activators of CDK (cyclin‐dependent kinase)–cyclin complexes to regulate progression through the CDC. We have recently identified a pool of CDC25B at the centrosome of interphase cells that plays a role in regulating centrosome numbers.</p>
<p><i>Results</i>
. In the present study, we demonstrate that CDC25B forms a close association with Ctn (centrin) proteins at the centrosome. This interaction involves both N‐ and C‐terminal regions of CDC25B and requires CDC25B binding to its CDK—cyclin substrates. However, the interaction is not dependent on the enzyme activity of CDC25B. Although CDC25B appears to bind indirectly to Ctn2, this association is pertinent to CDC25B localization at the centrosome. We further demonstrate that CDC25B plays a role in maintaining the overall integrity of the centrosome, by regulating the centrosome levels of multiple centrosome proteins, including that of Ctn2.</p>
<p><i>Conclusions</i>
. Our results therefore suggest that CDC25B associates with a Ctn2‐containing multiprotein complex in the cytoplasm, which targets it to the centrosome, where it plays a role in maintaining the centrosome levels of Ctn2 and a number of other centrosome components.</p>
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<titleInfo type="alternative" contentType="CDATA" lang="en"><title>CDC25B associates with a centrin 2‐containing complex and is involved in maintaining centrosome integrity</title>
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<name type="personal"><namePart type="given">Rose</namePart>
<namePart type="family">Boutros</namePart>
<affiliation>Diamantina Institute, Princess Alexandra Hospital, The University of Queensland, Brisbane, Australia</affiliation>
<affiliation>Université de Toulouse, LBCMCP, 118 route de Narbonne, F‐31062 Toulouse, France</affiliation>
<affiliation>E-mail: bernard.ducommun@itav‐recherche.fr</affiliation>
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</name>
<name type="personal"><namePart type="given">Corinne</namePart>
<namePart type="family">Lorenzo</namePart>
<affiliation>Université de Toulouse, LBCMCP, 118 route de Narbonne, F‐31062 Toulouse, France</affiliation>
<affiliation>Centre National de la Recherche Scientifique (CNRS), LBCMCP‐UMR5088, F‐31062 Toulouse, France</affiliation>
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</name>
<name type="personal"><namePart type="given">Odile</namePart>
<namePart type="family">Mondesert</namePart>
<affiliation>Université de Toulouse, LBCMCP, 118 route de Narbonne, F‐31062 Toulouse, France</affiliation>
<affiliation>Centre National de la Recherche Scientifique (CNRS), LBCMCP‐UMR5088, F‐31062 Toulouse, France</affiliation>
<role><roleTerm type="text">author</roleTerm>
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</name>
<name type="personal"><namePart type="given">Alain</namePart>
<namePart type="family">Jauneau</namePart>
<affiliation>CNRS, Plateforme Imagerie, Pôle de Biotechnologie Végétale, F‐31320 Castanet Tolosan, France</affiliation>
<role><roleTerm type="text">author</roleTerm>
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<name type="personal"><namePart type="given">Vanessa</namePart>
<namePart type="family">Oakes</namePart>
<affiliation>Diamantina Institute, Princess Alexandra Hospital, The University of Queensland, Brisbane, Australia</affiliation>
<role><roleTerm type="text">author</roleTerm>
</role>
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<name type="personal"><namePart type="given">Christine</namePart>
<namePart type="family">Dozier</namePart>
<affiliation>Université de Toulouse, LBCMCP, 118 route de Narbonne, F‐31062 Toulouse, France</affiliation>
<affiliation>Centre National de la Recherche Scientifique (CNRS), LBCMCP‐UMR5088, F‐31062 Toulouse, France</affiliation>
<role><roleTerm type="text">author</roleTerm>
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<name type="personal"><namePart type="given">Brian</namePart>
<namePart type="family">Gabrielli</namePart>
<affiliation>Diamantina Institute, Princess Alexandra Hospital, The University of Queensland, Brisbane, Australia</affiliation>
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<name type="personal"><namePart type="given">Bernard</namePart>
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<affiliation>Université de Toulouse, LBCMCP, 118 route de Narbonne, F‐31062 Toulouse, France</affiliation>
<affiliation>Centre National de la Recherche Scientifique (CNRS), LBCMCP‐UMR5088, F‐31062 Toulouse, France</affiliation>
<affiliation>CHU Purpan, Service d'Hématologie, TSA 40031, F‐31059 Toulouse, France</affiliation>
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<edition>Received 19 November 2010; Accepted 23 November 2010</edition>
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<abstract lang="en">Background information. CDC25 (cell division cycle 25) phosphatases function as activators of CDK (cyclin‐dependent kinase)–cyclin complexes to regulate progression through the CDC. We have recently identified a pool of CDC25B at the centrosome of interphase cells that plays a role in regulating centrosome numbers. Results. In the present study, we demonstrate that CDC25B forms a close association with Ctn (centrin) proteins at the centrosome. This interaction involves both N‐ and C‐terminal regions of CDC25B and requires CDC25B binding to its CDK—cyclin substrates. However, the interaction is not dependent on the enzyme activity of CDC25B. Although CDC25B appears to bind indirectly to Ctn2, this association is pertinent to CDC25B localization at the centrosome. We further demonstrate that CDC25B plays a role in maintaining the overall integrity of the centrosome, by regulating the centrosome levels of multiple centrosome proteins, including that of Ctn2. Conclusions. Our results therefore suggest that CDC25B associates with a Ctn2‐containing multiprotein complex in the cytoplasm, which targets it to the centrosome, where it plays a role in maintaining the centrosome levels of Ctn2 and a number of other centrosome components.</abstract>
<subject lang="en"><genre>keywords</genre>
<topic>CDC25B</topic>
<topic>centrin (Ctn)</topic>
<topic>centrosome</topic>
<topic>cyclin‐dependent kinase (CDK)</topic>
<topic>fluorescence lifetime imaging microscopy (FLIM)</topic>
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<part><date>2011</date>
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