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      LUBAC controls chromosome alignment by targeting CENP-E to attached kinetochores

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          Abstract

          Faithful chromosome segregation requires proper chromosome congression at prometaphase and dynamic maintenance of the aligned chromosomes at metaphase. Chromosome missegregation can result in aneuploidy, birth defects and cancer. The kinetochore-bound KMN network and the kinesin motor CENP-E are critical for kinetochore-microtubule attachment and chromosome stability. The linear ubiquitin chain assembly complex (LUBAC) attaches linear ubiquitin chains to substrates, with well-established roles in immune response. Here, we identify LUBAC as a key player of chromosome alignment during mitosis. LUBAC catalyzes linear ubiquitination of the kinetochore motor CENP-E, which is specifically required for the localization of CENP-E at attached kinetochores, but not unattached ones. KNL1 acts as a receptor of linear ubiquitin chains to anchor CENP-E at attached kinetochores in prometaphase and metaphase. Thus, linear ubiquitination promotes chromosome congression and dynamic chromosome alignment by coupling the dynamic kinetochore microtubule receptor CENP-E to the static one, the KMN network.

          Abstract

          During cell division, faithful chromosome segregation requires proper chromosome congression and dynamic maintenance of the aligned chromosomes. Here, the authors find that LUBAC promotes dynamic chromosome congression and alignment by targeting kinetochore motor CENP-E to the KMN network.

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          The conserved KMN network constitutes the core microtubule-binding site of the kinetochore.

          Iain M Cheeseman, Joshua S Chappie, Elizabeth M Wilson-Kubalek … (2006)
          The microtubule-binding interface of the kinetochore is of central importance in chromosome segregation. Although kinetochore components that stabilize, translocate on, and affect the polymerization state of microtubules have been identified, none have proven essential for kinetochore-microtubule interactions. Here, we examined the conserved KNL-1/Mis12 complex/Ndc80 complex (KMN) network, which is essential for kinetochore-microtubule interactions in vivo. We identified two distinct microtubule-binding activities within the KMN network: one associated with the Ndc80/Nuf2 subunits of the Ndc80 complex, and a second in KNL-1. Formation of the complete KMN network, which additionally requires the Mis12 complex and the Spc24/Spc25 subunits of the Ndc80 complex, synergistically enhances microtubule-binding activity. Phosphorylation by Aurora B, which corrects improper kinetochore-microtubule connections in vivo, reduces the affinity of the Ndc80 complex for microtubules in vitro. Based on these findings, we propose that the conserved KMN network constitutes the core microtubule-binding site of the kinetochore.
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            SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis.

            Fumiyo Ikeda, Yonathan Lissanu Deribe, Sigrid Skånland … (2011)
            SHARPIN is a ubiquitin-binding and ubiquitin-like-domain-containing protein which, when mutated in mice, results in immune system disorders and multi-organ inflammation. Here we report that SHARPIN functions as a novel component of the linear ubiquitin chain assembly complex (LUBAC) and that the absence of SHARPIN causes dysregulation of NF-κB and apoptotic signalling pathways, explaining the severe phenotypes displayed by chronic proliferative dermatitis (cpdm) in SHARPIN-deficient mice. Upon binding to the LUBAC subunit HOIP (also known as RNF31), SHARPIN stimulates the formation of linear ubiquitin chains in vitro and in vivo. Coexpression of SHARPIN and HOIP promotes linear ubiquitination of NEMO (also known as IKBKG), an adaptor of the IκB kinases (IKKs) and subsequent activation of NF-κB signalling, whereas SHARPIN deficiency in mice causes an impaired activation of the IKK complex and NF-κB in B cells, macrophages and mouse embryonic fibroblasts (MEFs). This effect is further enhanced upon concurrent downregulation of HOIL-1L (also known as RBCK1), another HOIP-binding component of LUBAC. In addition, SHARPIN deficiency leads to rapid cell death upon tumour-necrosis factor α (TNF-α) stimulation via FADD- and caspase-8-dependent pathways. SHARPIN thus activates NF-κB and inhibits apoptosis via distinct pathways in vivo.
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              Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions.

              Koraljka Husnjak, Ivan Dikic (2012)
              Ubiquitin acts as a versatile cellular signal that controls a wide range of biological processes including protein degradation, DNA repair, endocytosis, autophagy, transcription, immunity, and inflammation. The specificity of ubiquitin signaling is achieved by alternative conjugation signals (monoubiquitin and ubiquitin chains) and interactions with ubiquitin-binding proteins (known as ubiquitin receptors) that decode ubiquitinated target signals into biochemical cascades in the cell. Herein, we review the current knowledge pertaining to the structural and functional features of ubiquitin-binding proteins and the mechanisms by which they recognize various types of ubiquitin topologies. The combinatorial use of diverse ubiquitin-binding domains (UBDs) in full-length proteins, selective recognition of chains with distinct linkages and length, and posttranslational modifications of ubiquitin receptors or multivalent interactions within protein complexes illustrate a few mechanisms by which a circuitry of signaling networks can be rewired by ubiquitin-binding proteins to control cellular functions in vivo.
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                Author and article information

                Contributors
                Xuemin Zhang:
                ORCID: http://orcid.org/0000-0003-0207-4532
                zhangxuemin@cashq.ac.cn
                Huiyan Li: hyli@ncba.ac.cn
                Journal
                Journal ID (nlm-ta): Nat Commun
                Journal ID (iso-abbrev): Nat Commun
                Title: Nature Communications
                Publisher: Nature Publishing Group UK (London )
                ISSN (Electronic): 2041-1723
                Publication date (Electronic): 17 January 2019
                Publication date PMC-release: 17 January 2019
                Publication date Collection: 2019
                Volume: 10
                Electronic Location Identifier: 273
                Affiliations
                [1 ]GRID grid.410601.2, State Key Laboratory of Proteomics, , National Center of Biomedical Analysis, ; 100850 Beijing, China
                [2 ]ISNI 0000 0000 9889 6335, GRID grid.413106.1, Department of Radiation Oncology, National Cancer Center/Cancer Hospital, , Chinese Academy of Medical Sciences and Peking Union Medical College, ; 100021 Beijing, China
                [3 ]ISNI 0000 0004 1803 4911, GRID grid.410740.6, State Key Laboratory of Toxicology and Medical Countermeasures, , Beijing Institute of Pharmacology and Toxicology, ; 100850 Beijing, China
                [4 ]ISNI 0000 0004 0372 2033, GRID grid.258799.8, Department of Molecular and Cellular Physiology, Graduate School of Medicine, , Kyoto University, ; Yoshida-konoe-cho, Sakyo-ku, Kyoto, 606-8501 Japan
                [5 ]ISNI 0000 0001 0125 2443, GRID grid.8547.e, School of Basic Medical Sciences, , Fudan University, ; 200032 Shanghai, China
                Author information
                http://orcid.org/0000-0003-0207-4532
                Article
                Publisher ID: 8043
                DOI: 10.1038/s41467-018-08043-7
                PMC ID: 6336796
                PubMed ID: 30655516
                SO-VID: 70b9e20f-b74a-439c-93d2-e5d3b915411e
                Copyright © © The Author(s) 2019
                License:

                Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

                History
                Date received : 30 March 2018
                Date accepted : 7 December 2018
                Categories
                Subject: Article
                Custom metadata
                issue-copyright-statement © The Author(s) 2019

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