Academic Journal
Προβολή σε EDS

The interaction between RPAP3 and TRBP reveals a possible involvement of the HSP90/R2TP chaperone complex in the regulation of miRNA activity

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: The interaction between RPAP3 and TRBP reveals a possible involvement of the HSP90/R2TP chaperone complex in the regulation of miRNA activity
Συγγραφείς: Abel, Yoann, Charron, Christophe, Virciglio, Camille, Bourguignon-Igel, Valérie, Quinternet, Marc, Chagot, Marie-Eve, Robert, Marie-Cécile, Verheggen, Céline, Branlant, Christiane, Bertrand, Edouard, Manival, Xavier, Charpentier, Bruno, Rederstorff, Mathieu
Συνεισφορές: Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique Moléculaire de Montpellier (IGMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Ingénierie, Biologie et Santé en Lorraine (IBSLor), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Institut de génétique humaine (IGH), ANR-16-CE11-0032,snoRNPASSEMBLY,Comprendre l'assemblage des complexes macro-moléculaires en utilisant les snoRNP C/D comme modèle(2016)
Πηγή: ISSN: 0305-1048.
Στοιχεία εκδότη: CCSD
Oxford University Press
Έτος έκδοσης: 2022
Συλλογή: Inserm: HAL (Institut national de la santé et de la recherche médicale)
Θεματικοί όροι: [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
Περιγραφή: International audience ; MicroRNAs silence mRNAs by guiding the RISC complex. RISC assembly occurs following cleavage of pre-miRNAs by Dicer, assisted by TRBP or PACT, and the transfer of miRNAs to AGO proteins. The R2TP complex is an HSP90 co-chaperone involved in the assembly of ribonucleoprotein particles. Here, we show that the R2TP component RPAP3 binds TRBP but not PACT. The RPAP3-TPR1 domain interacts with the TRBP-dsRBD3, and the 1.5Å resolution crystal structure of this complex identifies key residues involved in the interaction. Remarkably, binding of TRBP to RPAP3 or Dicer is mutually exclusive. Additionally, we found that AGO(1/2), TRBP and Dicer are all sensitive to HSP90 inhibition, and that TRBP sensitivity is increased in the absence of RPAP3. Finally, RPAP3 seems to impede miRNA activity, raising the possibility that the R2TP chaperone might sequester TRBP to regulate the miRNA pathway.
Τύπος εγγράφου: article in journal/newspaper
Γλώσσα: English
Relation: info:eu-repo/semantics/altIdentifier/pmid/35150569; PUBMED: 35150569; PUBMEDCENTRAL: PMC8887487
DOI: 10.1093/nar/gkac086
Διαθεσιμότητα: https://hal.univ-lorraine.fr/hal-03583324
https://hal.univ-lorraine.fr/hal-03583324v1/document
https://hal.univ-lorraine.fr/hal-03583324v1/file/gkac086%2811%29.pdf
https://doi.org/10.1093/nar/gkac086
Rights: https://creativecommons.org/licenses/by-nc/4.0/ ; info:eu-repo/semantics/OpenAccess
Αριθμός Καταχώρησης: edsbas.3F04489
Βάση Δεδομένων: BASE
FullText Text:
  Availability: 0
CustomLinks:
  – Url: https://hal.univ-lorraine.fr/hal-03583324#
    Name: EDS - BASE (ns324271)
    Category: fullText
    Text: View record from BASE
Header DbId: edsbas
DbLabel: BASE
An: edsbas.3F04489
RelevancyScore: 920
AccessLevel: 3
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 920.2763671875
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: The interaction between RPAP3 and TRBP reveals a possible involvement of the HSP90/R2TP chaperone complex in the regulation of miRNA activity
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Abel%2C+Yoann%22">Abel, Yoann</searchLink><br /><searchLink fieldCode="AR" term="%22Charron%2C+Christophe%22">Charron, Christophe</searchLink><br /><searchLink fieldCode="AR" term="%22Virciglio%2C+Camille%22">Virciglio, Camille</searchLink><br /><searchLink fieldCode="AR" term="%22Bourguignon-Igel%2C+Valérie%22">Bourguignon-Igel, Valérie</searchLink><br /><searchLink fieldCode="AR" term="%22Quinternet%2C+Marc%22">Quinternet, Marc</searchLink><br /><searchLink fieldCode="AR" term="%22Chagot%2C+Marie-Eve%22">Chagot, Marie-Eve</searchLink><br /><searchLink fieldCode="AR" term="%22Robert%2C+Marie-Cécile%22">Robert, Marie-Cécile</searchLink><br /><searchLink fieldCode="AR" term="%22Verheggen%2C+Céline%22">Verheggen, Céline</searchLink><br /><searchLink fieldCode="AR" term="%22Branlant%2C+Christiane%22">Branlant, Christiane</searchLink><br /><searchLink fieldCode="AR" term="%22Bertrand%2C+Edouard%22">Bertrand, Edouard</searchLink><br /><searchLink fieldCode="AR" term="%22Manival%2C+Xavier%22">Manival, Xavier</searchLink><br /><searchLink fieldCode="AR" term="%22Charpentier%2C+Bruno%22">Charpentier, Bruno</searchLink><br /><searchLink fieldCode="AR" term="%22Rederstorff%2C+Mathieu%22">Rederstorff, Mathieu</searchLink>
– Name: Author
  Label: Contributors
  Group: Au
  Data: Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA)<br />Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS)<br />Institut de Génétique Moléculaire de Montpellier (IGMM)<br />Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)<br />Ingénierie, Biologie et Santé en Lorraine (IBSLor)<br />Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS)<br />Institut de génétique humaine (IGH)<br />ANR-16-CE11-0032,snoRNPASSEMBLY,Comprendre l'assemblage des complexes macro-moléculaires en utilisant les snoRNP C/D comme modèle(2016)
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <i>ISSN: 0305-1048</i>.
– Name: Publisher
  Label: Publisher Information
  Group: PubInfo
  Data: CCSD<br />Oxford University Press
– Name: DatePubCY
  Label: Publication Year
  Group: Date
  Data: 2022
– Name: Subset
  Label: Collection
  Group: HoldingsInfo
  Data: Inserm: HAL (Institut national de la santé et de la recherche médicale)
– Name: Subject
  Label: Subject Terms
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22[SDV%2EBBM]Life+Sciences+[q-bio]%2FBiochemistry%22">[SDV.BBM]Life Sciences [q-bio]/Biochemistry</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+Biology%22">Molecular Biology</searchLink>
– Name: Abstract
  Label: Description
  Group: Ab
  Data: International audience ; MicroRNAs silence mRNAs by guiding the RISC complex. RISC assembly occurs following cleavage of pre-miRNAs by Dicer, assisted by TRBP or PACT, and the transfer of miRNAs to AGO proteins. The R2TP complex is an HSP90 co-chaperone involved in the assembly of ribonucleoprotein particles. Here, we show that the R2TP component RPAP3 binds TRBP but not PACT. The RPAP3-TPR1 domain interacts with the TRBP-dsRBD3, and the 1.5Å resolution crystal structure of this complex identifies key residues involved in the interaction. Remarkably, binding of TRBP to RPAP3 or Dicer is mutually exclusive. Additionally, we found that AGO(1/2), TRBP and Dicer are all sensitive to HSP90 inhibition, and that TRBP sensitivity is increased in the absence of RPAP3. Finally, RPAP3 seems to impede miRNA activity, raising the possibility that the R2TP chaperone might sequester TRBP to regulate the miRNA pathway.
– Name: TypeDocument
  Label: Document Type
  Group: TypDoc
  Data: article in journal/newspaper
– Name: Language
  Label: Language
  Group: Lang
  Data: English
– Name: NoteTitleSource
  Label: Relation
  Group: SrcInfo
  Data: info:eu-repo/semantics/altIdentifier/pmid/35150569; PUBMED: 35150569; PUBMEDCENTRAL: PMC8887487
– Name: DOI
  Label: DOI
  Group: ID
  Data: 10.1093/nar/gkac086
– Name: URL
  Label: Availability
  Group: URL
  Data: https://hal.univ-lorraine.fr/hal-03583324<br />https://hal.univ-lorraine.fr/hal-03583324v1/document<br />https://hal.univ-lorraine.fr/hal-03583324v1/file/gkac086%2811%29.pdf<br />https://doi.org/10.1093/nar/gkac086
– Name: Copyright
  Label: Rights
  Group: Cpyrght
  Data: https://creativecommons.org/licenses/by-nc/4.0/ ; info:eu-repo/semantics/OpenAccess
– Name: AN
  Label: Accession Number
  Group: ID
  Data: edsbas.3F04489
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=edsbas&AN=edsbas.3F04489
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1093/nar/gkac086
    Languages:
      – Text: English
    Subjects:
      – SubjectFull: [SDV.BBM]Life Sciences [q-bio]/Biochemistry
        Type: general
      – SubjectFull: Molecular Biology
        Type: general
    Titles:
      – TitleFull: The interaction between RPAP3 and TRBP reveals a possible involvement of the HSP90/R2TP chaperone complex in the regulation of miRNA activity
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Abel, Yoann
      – PersonEntity:
          Name:
            NameFull: Charron, Christophe
      – PersonEntity:
          Name:
            NameFull: Virciglio, Camille
      – PersonEntity:
          Name:
            NameFull: Bourguignon-Igel, Valérie
      – PersonEntity:
          Name:
            NameFull: Quinternet, Marc
      – PersonEntity:
          Name:
            NameFull: Chagot, Marie-Eve
      – PersonEntity:
          Name:
            NameFull: Robert, Marie-Cécile
      – PersonEntity:
          Name:
            NameFull: Verheggen, Céline
      – PersonEntity:
          Name:
            NameFull: Branlant, Christiane
      – PersonEntity:
          Name:
            NameFull: Bertrand, Edouard
      – PersonEntity:
          Name:
            NameFull: Manival, Xavier
      – PersonEntity:
          Name:
            NameFull: Charpentier, Bruno
      – PersonEntity:
          Name:
            NameFull: Rederstorff, Mathieu
      – PersonEntity:
          Name:
            NameFull: Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA)
      – PersonEntity:
          Name:
            NameFull: Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS)
      – PersonEntity:
          Name:
            NameFull: Institut de Génétique Moléculaire de Montpellier (IGMM)
      – PersonEntity:
          Name:
            NameFull: Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)
      – PersonEntity:
          Name:
            NameFull: Ingénierie, Biologie et Santé en Lorraine (IBSLor)
      – PersonEntity:
          Name:
            NameFull: Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS)
      – PersonEntity:
          Name:
            NameFull: Institut de génétique humaine (IGH)
      – PersonEntity:
          Name:
            NameFull: ANR-16-CE11-0032,snoRNPASSEMBLY,Comprendre l'assemblage des complexes macro-moléculaires en utilisant les snoRNP C/D comme modèle(2016)
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 01
              M: 01
              Type: published
              Y: 2022
          Identifiers:
            – Type: issn-locals
              Value: edsbas
            – Type: issn-locals
              Value: edsbas.oa
          Titles:
            – TitleFull: ISSN: 0305-1048
              Type: main
ResultId 1