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      The role of cullin 5-containing ubiquitin ligases

      review-article
      Author(s): , , ,
      Publication date (Electronic):
      Journal: Cell Division
      Publisher: BioMed Central
      Keywords: Ubiquitin, Cullin 5, Elongin, CRL complex

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          Abstract

          The suppressor of cytokine signaling (SOCS) box consists of the BC box and the cullin 5 (Cul5) box, which interact with Elongin BC and Cul5, respectively. SOCS box-containing proteins have ubiquitin ligase activity mediated by the formation of a complex with the scaffold protein Cul5 and the RING domain protein Rbx2, and are thereby members of the cullin RING ligase superfamily. Cul5-type ubiquitin ligases have a variety of substrates that are targeted for polyubiquitination and proteasomal degradation. Here, we review the current knowledge on the identification of Cul5 and the regulation of its expression, as well as the signaling pathways regulated by Cul5 and how viruses highjack the Cul5 system to overcome antiviral responses.

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          DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival.

          Timothy Peterson, Mathieu Laplante, Carson C. Thoreen … (2009)
          The mTORC1 and mTORC2 pathways regulate cell growth, proliferation, and survival. We identify DEPTOR as an mTOR-interacting protein whose expression is negatively regulated by mTORC1 and mTORC2. Loss of DEPTOR activates S6K1, Akt, and SGK1, promotes cell growth and survival, and activates mTORC1 and mTORC2 kinase activities. DEPTOR overexpression suppresses S6K1 but, by relieving feedback inhibition from mTORC1 to PI3K signaling, activates Akt. Consistent with many human cancers having activated mTORC1 and mTORC2 pathways, DEPTOR expression is low in most cancers. Surprisingly, DEPTOR is highly overexpressed in a subset of multiple myelomas harboring cyclin D1/D3 or c-MAF/MAFB translocations. In these cells, high DEPTOR expression is necessary to maintain PI3K and Akt activation and a reduction in DEPTOR levels leads to apoptosis. Thus, we identify a novel mTOR-interacting protein whose deregulated overexpression in multiple myeloma cells represents a mechanism for activating PI3K/Akt signaling and promoting cell survival.
          Article 0 comments Cited 412 times – based on 0 reviews     Review now
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            Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition.

            Mikko Taipale, Irina Krykbaeva, Martina Koeva … (2012)
            HSP90 is a molecular chaperone that associates with numerous substrate proteins called clients. It plays many important roles in human biology and medicine, but determinants of client recognition by HSP90 have remained frustratingly elusive. We systematically and quantitatively surveyed most human kinases, transcription factors, and E3 ligases for interaction with HSP90 and its cochaperone CDC37. Unexpectedly, many more kinases than transcription factors bound HSP90. CDC37 interacted with kinases, but not with transcription factors or E3 ligases. HSP90::kinase interactions varied continuously over a 100-fold range and provided a platform to study client protein recognition. In wild-type clients, HSP90 did not bind particular sequence motifs, but rather associated with intrinsically unstable kinases. Stabilization of the kinase in either its active or inactive conformation with diverse small molecules decreased HSP90 association. Our results establish HSP90 client recognition as a combinatorial process: CDC37 provides recognition of the kinase family, whereas thermodynamic parameters determine client binding within the family. Copyright © 2012 Elsevier Inc. All rights reserved.
            Article 0 comments Cited 317 times – based on 0 reviews     Review now
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              Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation.

              David M Duda, Laura Borg, Daniel Scott … (2008)
              Cullin-RING ligases (CRLs) comprise the largest ubiquitin E3 subclass, in which a central cullin subunit links a substrate-binding adaptor with an E2-binding RING. Covalent attachment of the ubiquitin-like protein NEDD8 to a conserved C-terminal domain (ctd) lysine stimulates CRL ubiquitination activity and prevents binding of the inhibitor CAND1. Here we report striking conformational rearrangements in the crystal structure of NEDD8~Cul5(ctd)-Rbx1 and SAXS analysis of NEDD8~Cul1(ctd)-Rbx1 relative to their unmodified counterparts. In NEDD8ylated CRL structures, the cullin WHB and Rbx1 RING subdomains are dramatically reoriented, eliminating a CAND1-binding site and imparting multiple potential catalytic geometries to an associated E2. Biochemical analyses indicate that the structural malleability is important for both CRL NEDD8ylation and subsequent ubiquitination activities. Thus, our results point to a conformational control of CRL activity, with ligation of NEDD8 shifting equilibria to disfavor inactive CAND1-bound closed architectures, and favor dynamic, open forms that promote polyubiquitination.
              Article 0 comments Cited 267 times – based on 0 reviews     Review now
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                Author and article information

                Contributors
                Fumihiko Okumura: +81-52-789-2988 , okumura.fumihiko@a.mbox.nagoya-u.ac.jp
                Akiko Joo-Okumura: okumura.akiko@d.mbox.nagoya-u.ac.jp
                Kunio Nakatsukasa: z47875a@cc.nagoya-u.ac.jp
                Takumi Kamura: z47617a@nucc.cc.nagoya-u.ac.jp
                Journal
                Journal ID (nlm-ta): Cell Div
                Journal ID (iso-abbrev): Cell Div
                Title: Cell Division
                Publisher: BioMed Central (London )
                ISSN (Electronic): 1747-1028
                Publication date (Electronic): 9 March 2016
                Publication date PMC-release: 9 March 2016
                Publication date Collection: 2016
                Volume: 11
                Electronic Location Identifier: 1
                Affiliations
                Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Aichi 464-8602 Japan
                Article
                Publisher ID: 16
                DOI: 10.1186/s13008-016-0016-3
                PMC ID: 4812663
                PubMed ID: 27030794
                SO-VID: 2fabaa87-0af3-4b0d-ba2e-59477ccac6ee
                Copyright © © Okumura et al. 2016
                License:

                Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

                History
                Date received : 28 January 2016
                Date accepted : 2 March 2016
                Funding
                Funded by: JSPS KAKENHI
                Award ID: 25291023
                Award ID: 25860043
                Award ID: 24112006
                Award Recipient :
                Categories
                Subject: Review
                Custom metadata
                issue-copyright-statement © The Author(s) 2016

                ScienceOpen disciplines: Cell biology
                Keywords: ubiquitin,cullin 5,elongin,crl complex
                Data availability:
                ScienceOpen disciplines: Cell biology
                Keywords: ubiquitin, cullin 5, elongin, crl complex

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