We are analyzing https://link.springer.com/chapter/10.1007/978-981-15-1025-0_2.

Title:
Structural Biology of CRL Ubiquitin Ligases | SpringerLink
Description:
Cullin-RING ubiquitin ligases (CRLs) represent the largest superfamily of multi-subunit E3s conserved in all eukaryotes. Soon after the discovery of these important ubiquitin ligase machineries, structural studies have made tremendous contributions to our...
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Keywords {🔍}

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Topics {✒️}

thiol-based sensor-effector apparatus beta-trcp1-skp1-beta-catenin complex inositol-phosphate-potentiated coi1-jaz pro/n-end rule pathway ubiquitin-conjugating enzyme e2 hiv-1 vif-cul5-scf complex cullin–ring e3 networks month download article/chapter vhl-elobc-cul2 complex btb-cul3 ubiquitin ligases n-end rule pathway n-terminal acetylation acts diglycine c-end degron multi-subunit e3s conserved failed uga/sec decoding chapter cullin-ring ligases multi-subunit complexes assemble hif-1alpha -pvhl complex n-end rule substrates conserved protein dcn-1/dcn1p bric-a-brac cand1 p185/cul7 gene results glomulin-rbx1-cul1 complex vhl-elongin c-elongin hours mutant reveals btb/poz domain proteins scf ubiquitin-ligase complex thalidomide-dependent cereblon substrate ring e3 ligase f-box protein expression crl-substrate interactions regulated mammalian f-box proteins ring e3 trapped multisite-phosphorylated substrate recognition cullin-ring ligases lenalidomide-induced ck1α degradation c-terminal tail e3 ligases work versatile e3 platform vhl-mediated destruction lin hc harvard medical school privacy choices/manage cookies nrf2-dlgex degron wingless β-trcp transcription factor implicated mammalian circadian clock enchev ri device instant download modular ubiquitin ligase

Questions {❓}

Specifically, how do the CRL subunits interact with each other to form a versatile E3 platform?

Schema {🗺️}

ScholarlyArticle:
      headline:Structural Biology of CRL Ubiquitin Ligases
      pageEnd:31
      pageStart:9
      image:https://media.springernature.com/w153/springer-static/cover/book/978-981-15-1025-0.jpg
      genre:
         Biomedical and Life Sciences
         Biomedical and Life Sciences (R0)
      isPartOf:
         name:Cullin-RING Ligases and Protein Neddylation
         isbn:
            978-981-15-1025-0
            978-981-15-1024-3
         type:Book
      publisher:
         name:Springer Singapore
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Domnița-Valeria Rusnac
            affiliation:
                  name:University of Washington
                  address:
                     name:Department of Pharmacology, University of Washington, Seattle, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Ning Zheng
            affiliation:
                  name:University of Washington
                  address:
                     name:Department of Pharmacology, University of Washington, Seattle, USA
                     type:PostalAddress
                  type:Organization
                  name:Howard Hughes Medical Institute, University of Washington
                  address:
                     name:Howard Hughes Medical Institute, University of Washington, Seattle, USA
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      keywords:Cullin-RING ubiquitin ligases, Structural biology, Ubiquitination, Neddylation, DCN1
      description:Cullin-RING ubiquitin ligases (CRLs) represent the largest superfamily of multi-subunit E3s conserved in all eukaryotes. Soon after the discovery of these important ubiquitin ligase machineries, structural studies have made tremendous contributions to our understanding of their functions. Identification of the key components of CRLs by early studies raised immediate questions as to how these multi-subunit complexes assemble to promote the polyubiquitination of substrates. Specifically, how do the CRL subunits interact with each other to form a versatile E3 platform? How do they recognize specific substrates? How are the CRL-substrate interactions regulated in response to upstream signals? How are the CRL E3s themselves activated and deactivated, and how are substrate receptor subunits of CRLs exchanged in the cell? Even though we might not yet have complete answers to these questions, extensive structural analyses of CRL complexes in the past two decades have begun to unveil the themes and variations of CRL biology. In this chapter we will discuss both classic and emerging structures that help elucidate the overall architecture of CRLs, their substrate recognition modes, and regulatory mechanism of CRLs by NEDD8 modification.
      datePublished:2020
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      name:University of Washington
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      address:
         name:Department of Pharmacology, University of Washington, Seattle, USA
         type:PostalAddress
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            address:
               name:Department of Pharmacology, University of Washington, Seattle, USA
               type:PostalAddress
            type:Organization
      name:Ning Zheng
      affiliation:
            name:University of Washington
            address:
               name:Department of Pharmacology, University of Washington, Seattle, USA
               type:PostalAddress
            type:Organization
            name:Howard Hughes Medical Institute, University of Washington
            address:
               name:Howard Hughes Medical Institute, University of Washington, Seattle, USA
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      email:[email protected]
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      name:Howard Hughes Medical Institute, University of Washington, Seattle, USA
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