34
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Loss of mitochondrial peptidase Clpp leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors

      research-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The caseinolytic peptidase P (CLPP) is conserved from bacteria to humans. In the mitochondrial matrix, it multimerizes and forms a macromolecular proteasome-like cylinder together with the chaperone CLPX. In spite of a known relevance for the mitochondrial unfolded protein response, its substrates and tissue-specific roles are unclear in mammals. Recessive CLPP mutations were recently observed in the human Perrault variant of ovarian failure and sensorineural hearing loss. Here, a first characterization of CLPP null mice demonstrated complete female and male infertility and auditory deficits. Disrupted spermatogenesis already at the spermatid stage and ovarian follicular differentiation failure were evident. Reduced pre-/post-natal survival and marked ubiquitous growth retardation contrasted with only light impairment of movement and respiratory activities. Interestingly, the mice showed resistance to ulcerative dermatitis. Systematic expression studies detected up-regulation of other mitochondrial chaperones, accumulation of CLPX and mtDNA as well as inflammatory factors throughout tissues. T-lymphocytes in the spleen were activated. Thus, murine Clpp deletion represents a faithful Perrault model. The disease mechanism probably involves deficient clearance of mitochondrial components and inflammatory tissue destruction.

          Related collections

          Most cited references86

          • Record: found
          • Abstract: not found
          • Article: not found

          Controlling the False Discovery Rate: A Practical and Powerful Approach to Multiple Testing

            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment.

            Mutations in phosphatase and tensin homologue-induced kinase 1 (PINK1) cause recessively inherited Parkinson's disease (PD), a neurodegenerative disorder linked to mitochondrial dysfunction. In healthy mitochondria, PINK1 is rapidly degraded in a process involving both mitochondrial proteases and the proteasome. However, when mitochondrial import is compromised by depolarization, PINK1 accumulates on the mitochondrial surface where it recruits the PD-linked E3 ubiquitin ligase Parkin from the cytosol, which in turn mediates the autophagic destruction of the dysfunctional organelles. Using an unbiased RNA-mediated interference (RNAi)-based screen, we identified four mitochondrial proteases, mitochondrial processing peptidase (MPP), presenilin-associated rhomboid-like protease (PARL), m-AAA and ClpXP, involved in PINK1 degradation. We find that PINK1 turnover is particularly sensitive to even modest reductions in MPP levels. Moreover, PINK1 cleavage by MPP is coupled to import such that reducing MPP activity induces PINK1 accumulation at the mitochondrial surface, leading to Parkin recruitment and mitophagy. These results highlight a new role for MPP in PINK1 import and mitochondrial quality control via the PINK1–Parkin pathway.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria.

              Mouse kif5B gene was disrupted by homologous recombination. kif5B-/- mice were embryonic lethal with a severe growth retardation at 9.5-11.5 days postcoitum. To analyze the significance of this conventional kinesin heavy chain in organelle transport, we studied the distribution of major organelles in the extraembryonic cells. The null mutant cells impaired lysosomal dispersion, while brefeldin A could normally induce the breakdown of their Golgi apparatus. More prominently, their mitochondria abnormally clustered in the perinuclear region. This mitochondrial phenotype was reversed by an exogenous expression of KIF5B, and a subcellular fractionation revealed that KIF5B is associated with mitochondria. These data collectively indicate that kinesin is essential for mitochondrial and lysosomal dispersion rather than for the Golgi-to-ER traffic in these cells.
                Bookmark

                Author and article information

                Contributors
                Journal
                Hum Mol Genet
                Hum. Mol. Genet
                hmg
                hmg
                Human Molecular Genetics
                Oxford University Press
                0964-6906
                1460-2083
                15 December 2013
                12 July 2013
                : 22
                : 24
                : 4871-4887
                Affiliations
                [1 ] Experimental Neurology,
                [2 ] Molecular Bioenergetics Group, Center of Biological Chemistry, Cluster of Excellence Macromolecular Complexes and
                [3 ] Edinger Institute (Neurological Institute), Goethe University Medical School , 60590 Frankfurt am Main, Germany
                [4 ] Institute of Human Genetics, Georg-August-University of Göttingen , 37073 Göttingen, Germany
                [5 ] Department of Genetics and Evolution, Jagiellonian University , 30-387 Kraków, Poland
                [6 ] Mitochondrial Biology, Buchmann Institute for Molecular Life Sciences and Mitochondrial Biology, Center for Molecular Medicine, Goethe University , 60438 Frankfurt am Main, Germany
                [7 ] Faculty for Biosciences, Molecular Developmental Biology, Cluster of Excellence Macromolecular Complexes, Goethe University , 60590 Frankfurt am Main, Germany
                [8 ] Institute for Medical Genetics and
                [9 ] Center for Bioinformatics Tuebingen (ZBIT), Eberhard-Karls-University of Tuebingen , 72076 Tübingen, Germany
                [10 ] German Mouse Clinic, Institute of Experimental Genetics, Helmholtz Zentrum München , München, Germany and
                [11 ] Institute for Medical Microbiology, Immunology and Hygiene, Technische Universität , München, Germany
                Author notes
                [* ]To whom correspondence should be addressed at: Experimental Neurology, Building 89, Goethe University Medical School, Theodor Stern Kai 7, 60590 Frankfurt am Main, Germany. Tel: +49 6963017428; Fax: +49 6963017128; Email: auburger@ 123456em.uni-frankfurt.de
                [†]

                Present address: Radboud University Nijmegen Medical Centre, Nijmegen Centre for Mitochondrial Disorders, Geert Groteplein-Zuid 10, 6525 GA Nijmegen, The Netherlands.

                Article
                ddt338
                10.1093/hmg/ddt338
                7108587
                23851121
                21dd00f5-3c10-45cc-9651-ca60f6179a8b
                © The Author 2013. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oup.com

                This article is made available via the PMC Open Access Subset for unrestricted re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the COVID-19 pandemic or until permissions are revoked in writing. Upon expiration of these permissions, PMC is granted a perpetual license to make this article available via PMC and Europe PMC, consistent with existing copyright protections.

                History
                : 4 June 2013
                : 9 July 2013
                Categories
                Articles

                Genetics
                Genetics

                Comments

                Comment on this article