ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
Collection
Publisher
Years
  • 1
    facet.materialart.
    Unknown
    The pseudokinase TRIB1 toggles an intramolecular switch to regulate COP1 nuclear export (2019)
    Springer Nature
    Details
    Publication Date: 2019
    Description: 〈p〉COP1 is a highly conserved ubiquitin ligase that regulates diverse cellular processes in plants and metazoans. Tribbles pseudokinases, which only exist in metazoans, act as scaffolds that interact with COP1 and its substrates to facilitate ubiquitination. Here, we report that, in addition to this scaffolding role, TRIB1 promotes nuclear localization of COP1 by disrupting an intramolecular interaction between the WD40 domain and a previously uncharacterized regulatory site within COP1. This site, which we have termed the pseudosubstrate latch (PSL), resembles the consensus COP1-binding motif present in known COP1 substrates. Our findings support a model in which binding of the PSL to the WD40 domain stabilizes a conformation of COP1 that is conducive to CRM1-mediated nuclear export, and TRIB1 displaces this intramolecular interaction to induce nuclear retention of COP1. Coevolution of Tribbles and the PSL in metazoans further underscores the importance of this role of Tribbles in regulating COP1 function.〈/p〉
    Print ISSN: 0261-4189
    Electronic ISSN: 1460-2075
    Topics: Biology , Medicine
    Published by Springer Nature on behalf of The European Molecular Biology Organization (EMBO).
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    facet.materialart.
    Unknown
    The pseudokinase TRIB1 toggles an intramolecular switch to regulate COP1 nuclear export (2019)
    Springer Nature
    Details
    Publication Date: 2019
    Description: 〈sec〉〈st〉Synopsis〈/st〉〈p〉〈textbox textbox-type="graphic"〉〈p〉〈inline-fig〉〈/inline-fig〉〈/p〉〈/textbox〉〈/p〉 〈p〉COP1 is a highly conserved E3 ubiquitin ligase that shuttles between the nucleus and cytoplasm. In plants, COP1 localization is controlled by light, while in metazoans, the pseudokinase TRIB1 promotes COP1 nuclear localization by competing with an intramolecular site that regulates CRM1-mediated nuclear export of COP1.〈/p〉 〈p〉 〈l type="unord"〉〈li〉〈p〉Binding of the TRIB1 C-terminal tail to the COP1 WD40 domain potentiates COP1 nuclear localization.〈/p〉〈/li〉 〈li〉〈p〉COP1 nucleocytoplasmic shuttling is controlled by an intramolecular site, termed the pseudosubstrate latch (PSL), that competes with TRIB1 for binding to the WD40 domain.〈/p〉〈/li〉 〈li〉〈p〉Disruption of the PSL/WD40 interaction through mutations or TRIB1 binding interferes with CRM1-mediated nuclear export of COP1.〈/p〉〈/li〉 〈li〉〈p〉Phylogenetic analysis indicates that the COP1-binding motifs in the TRIB1 tail and COP1 PSL coevolved in metazoan species.〈/p〉〈/li〉〈/l〉 〈/p〉〈/sec〉
    Print ISSN: 0261-4189
    Electronic ISSN: 1460-2075
    Topics: Biology , Medicine
    Published by Springer Nature on behalf of The European Molecular Biology Organization (EMBO).
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...