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Journal articles on the topic 'AFG3L2'

Author: Grafiati

Published: 10 March 2023

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1

Koppen, Mirko, Florian Bonn, Sarah Ehses, and Thomas Langer. "Autocatalytic Processing of m-AAA Protease Subunits in Mitochondria." Molecular Biology of the Cell 20, no. 19 (October 2009): 4216–24. http://dx.doi.org/10.1091/mbc.e09-03-0218.

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m-AAA proteases are ATP-dependent proteolytic machines in the inner membrane of mitochondria which are crucial for the maintenance of mitochondrial activities. Conserved nuclear-encoded subunits, termed paraplegin, Afg3l1, and Afg3l2, form various isoenzymes differing in their subunit composition in mammalian mitochondria. Mutations in different m-AAA protease subunits are associated with distinct neuronal disorders in human. However, the biogenesis of m-AAA protease complexes or of individual subunits is only poorly understood. Here, we have examined the processing of nuclear-encoded m-AAA protease subunits upon import into mitochondria and demonstrate autocatalytic processing of Afg3l1 and Afg3l2. The mitochondrial processing peptidase MPP generates an intermediate form of Afg3l2 that is matured autocatalytically. Afg3l1 or Afg3l2 are also required for maturation of newly imported paraplegin subunits after their cleavage by MPP. Our results establish that mammalian m-AAA proteases can act as processing enzymes in vivo and reveal overlapping activities of Afg3l1 and Afg3l2. These findings might be of relevance for the pathogenesis of neurodegenerative disorders associated with mutations in different m-AAA protease subunits.

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2

Koppen, Mirko, Metodi D. Metodiev, Giorgio Casari, Elena I. Rugarli, and Thomas Langer. "Variable and Tissue-Specific Subunit Composition of Mitochondrial m-AAA Protease Complexes Linked to Hereditary Spastic Paraplegia." Molecular and Cellular Biology 27, no. 2 (November 13, 2006): 758–67. http://dx.doi.org/10.1128/mcb.01470-06.

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ABSTRACT The m-AAA protease, an ATP-dependent proteolytic complex in the mitochondrial inner membrane, controls protein quality and regulates ribosome assembly, thus exerting essential housekeeping functions within mitochondria. Mutations in the m-AAA protease subunit paraplegin cause axonal degeneration in hereditary spastic paraplegia (HSP), but the basis for the unexpected tissue specificity is not understood. Paraplegin assembles with homologous Afg3l2 subunits into hetero-oligomeric complexes which can substitute for yeast m-AAA proteases, demonstrating functional conservation. The function of a third paralogue, Afg3l1 expressed in mouse, is unknown. Here, we analyze the assembly of paraplegin into m-AAA complexes and monitor consequences of paraplegin deficiency in HSP fibroblasts and in a mouse model for HSP. Our findings reveal variability in the assembly of m-AAA proteases in mitochondria in different tissues. Homo-oligomeric Afg3l1 and Afg3l2 complexes and hetero-oligomeric assemblies of both proteins with paraplegin can be formed. Yeast complementation studies demonstrate the proteolytic activity of these assemblies. Paraplegin deficiency in HSP does not result in the loss of m-AAA protease activity in brain mitochondria. Rather, homo-oligomeric Afg3l2 complexes accumulate, and these complexes can substitute for housekeeping functions of paraplegin-containing m-AAA complexes. We therefore propose that the formation of m-AAA proteases with altered substrate specificities leads to axonal degeneration in HSP.

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Cesnekova, Jana, Marie Rodinova, Hana Hansikova, Jiri Zeman, and Lukas Stiburek. "Loss of Mitochondrial AAA Proteases AFG3L2 and YME1L Impairs Mitochondrial Structure and Respiratory Chain Biogenesis." International Journal of Molecular Sciences 19, no. 12 (December 7, 2018): 3930. http://dx.doi.org/10.3390/ijms19123930.

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Mitochondrial protein quality control is crucial for the maintenance of correct mitochondrial homeostasis. It is ensured by several specific mitochondrial proteases located across the various mitochondrial subcompartments. Here, we focused on characterization of functional overlap and cooperativity of proteolytic subunits AFG3L2 (AFG3 Like Matrix AAA Peptidase Subunit 2) and YME1L (YME1 like ATPase) of mitochondrial inner membrane AAA (ATPases Associated with diverse cellular Activities) complexes in the maintenance of mitochondrial structure and respiratory chain integrity. We demonstrate that loss of AFG3L2 and YME1L, both alone and in combination, results in diminished cell proliferation, fragmentation of mitochondrial reticulum, altered cristae morphogenesis, and defective respiratory chain biogenesis. The double AFG3L2/YME1L knockdown cells showed marked upregulation of OPA1 protein forms, with the most prominent increase in short OPA1 (optic atrophy 1). Loss of either protease led to marked elevation in OMA1 (OMA1 zinc metallopeptidase) (60 kDa) and severe reduction in the SPG7 (paraplegin) subunit of the m-AAA complex. Loss of the YME1L subunit led to an increased Drp1 level in mitochondrial fractions. While loss of YME1L impaired biogenesis and function of complex I, knockdown of AFG3L2 mainly affected the assembly and function of complex IV. Our results suggest cooperative and partly redundant functions of AFG3L2 and YME1L in the maintenance of mitochondrial structure and respiratory chain biogenesis and stress the importance of correct proteostasis for mitochondrial integrity.

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Ehses, Sarah, Ines Raschke, Giuseppe Mancuso, Andrea Bernacchia, Stefan Geimer, Daniel Tondera, Jean-Claude Martinou, Benedikt Westermann, Elena I. Rugarli, and Thomas Langer. "Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1." Journal of Cell Biology 187, no. 7 (December 28, 2009): 1023–36. http://dx.doi.org/10.1083/jcb.200906084.

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Mitochondrial fusion depends on the dynamin-like guanosine triphosphatase OPA1, whose activity is controlled by proteolytic cleavage. Dysfunction of mitochondria induces OPA1 processing and results in mitochondrial fragmentation, allowing the selective removal of damaged mitochondria. In this study, we demonstrate that two classes of metallopeptidases regulate OPA1 cleavage in the mitochondrial inner membrane: isoenzymes of the adenosine triphosphate (ATP)–dependent matrix AAA (ATPase associated with diverse cellular activities [m-AAA]) protease, variable assemblies of the conserved subunits paraplegin, AFG3L1 and -2, and the ATP-independent peptidase OMA1. Functionally redundant isoenzymes of the m-AAA protease ensure the balanced accumulation of long and short isoforms of OPA1 required for mitochondrial fusion. The loss of AFG3L2 in mouse tissues, down-regulation of AFG3L1 and -2 in mouse embryonic fibroblasts, or the expression of a dominant-negative AFG3L2 variant in human cells decreases the stability of long OPA1 isoforms and induces OPA1 processing by OMA1. Moreover, cleavage by OMA1 causes the accumulation of short OPA1 variants if mitochondrial DNA is depleted or mitochondrial activities are impaired. Our findings link distinct peptidases to constitutive and induced OPA1 processing and shed new light on the pathogenesis of neurodegenerative disorders associated with mutations in m-AAA protease subunits.

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5

Tulli, Susanna, Andrea Del Bondio, Valentina Baderna, Davide Mazza, Franca Codazzi, Tyler Mark Pierson, Alessandro Ambrosi, et al. "Pathogenic variants in the AFG3L2 proteolytic domain cause SCA28 through haploinsufficiency and proteostatic stress-driven OMA1 activation." Journal of Medical Genetics 56, no. 8 (March 25, 2019): 499–511. http://dx.doi.org/10.1136/jmedgenet-2018-105766.

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BackgroundSpinocerebellar ataxia type 28 (SCA28) is a dominantly inherited neurodegenerative disease caused by pathogenic variants in AFG3L2. The AFG3L2 protein is a subunit of mitochondrial m-AAA complexes involved in protein quality control. Objective of this study was to determine the molecular mechanisms of SCA28, which has eluded characterisation to date.MethodsWe derived SCA28 patient fibroblasts carrying different pathogenic variants in the AFG3L2 proteolytic domain (missense: the newly identified p.F664S and p.M666T, p.G671R, p.Y689H and a truncating frameshift p.L556fs) and analysed multiple aspects of mitochondrial physiology. As reference of residual m-AAA activity, we included SPAX5 patient fibroblasts with homozygous p.Y616C pathogenic variant, AFG3L2+/− HEK293 T cells by CRISPR/Cas9-genome editing and Afg3l2−/− murine fibroblasts.ResultsWe found that SCA28 cells carrying missense changes have normal levels of assembled m-AAA complexes, while the cells with a truncating pathogenic variant had only half of this amount. We disclosed inefficient mitochondrial fusion in SCA28 cells caused by increased OPA1 processing operated by hyperactivated OMA1. Notably, we found altered mitochondrial proteostasis to be the trigger of OMA1 activation in SCA28 cells, with pharmacological attenuation of mitochondrial protein synthesis resulting in stabilised levels of OMA1 and OPA1 long forms, which rescued mitochondrial fusion efficiency. Secondary to altered mitochondrial morphology, mitochondrial calcium uptake resulted decreased in SCA28 cells.ConclusionOur data identify the earliest events in SCA28 pathogenesis and open new perspectives for therapy. By identifying similar mitochondrial phenotypes between SCA28 cells and AFG3L2+/− cells, our results support haploinsufficiency as the mechanism for the studied pathogenic variants.

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Duvezin-Caubet, Stéphane, Mirko Koppen, Johannes Wagener, Michael Zick, Lars Israel, Andrea Bernacchia, Ravi Jagasia, et al. "OPA1 Processing Reconstituted in Yeast Depends on the Subunit Composition of the m-AAA Protease in Mitochondria." Molecular Biology of the Cell 18, no. 9 (September 2007): 3582–90. http://dx.doi.org/10.1091/mbc.e07-02-0164.

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The morphology of mitochondria in mammalian cells is regulated by proteolytic cleavage of OPA1, a dynamin-like GTPase of the mitochondrial inner membrane. The mitochondrial rhomboid protease PARL, and paraplegin, a subunit of the ATP-dependent m-AAA protease, were proposed to be involved in this process. Here, we characterized individual OPA1 isoforms by mass spectrometry, and we reconstituted their processing in yeast to identify proteases involved in OPA1 cleavage. The yeast homologue of OPA1, Mgm1, was processed both by PARL and its yeast homologue Pcp1. Neither of these rhomboid proteases cleaved OPA1. The formation of small OPA1 isoforms was impaired in yeast cells lacking the m-AAA protease subunits Yta10 and Yta12 and was restored upon expression of murine or human m-AAA proteases. OPA1 processing depended on the subunit composition of mammalian m-AAA proteases. Homo-oligomeric m-AAA protease complexes composed of murine Afg3l1, Afg3l2, or human AFG3L2 subunits cleaved OPA1 with higher efficiency than paraplegin-containing m-AAA proteases. OPA1 processing proceeded normally in murine cell lines lacking paraplegin or PARL. Our results provide evidence for different substrate specificities of m-AAA proteases composed of different subunits and reveal a striking evolutionary switch of proteases involved in the proteolytic processing of dynamin-like GTPases in mitochondria.

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7

Almomen, MM, KA Martens, A. Hanson, L. Korngut, and G. pfeffer. "P.071 Novel mutations in SPG7 identified from patients with late-onset spasticity." Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 45, s2 (June 2018): S35. http://dx.doi.org/10.1017/cjn.2018.173.

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Background: Hereditary spastic paraplegia (HSP) is a group of genetic diseases that cause progressive degeneration of the corticospinal tract. Historically, this disease was divided into two types:the classic subtype, with leg weakness and hypertonic bladder, and the complicated subtype, with features such as cerebellar ataxia or optic atrophy.Mutations in SPG7 (encoding paraplegin) leads to complicated HSP causing cerebellar ataxia, progressive external ophthalmoplegia in addition to the classical symptoms. AFG3L2 is a binding partner of paraplegin and mutations in AFG3L2 cause a similar syndrome Methods: From a neurogenetic clinic , we identified 11 patients with late-onset HSP. Sequencing of SPG7 and AFG3L2 was performed using a customised assay, and/or clinical diagnostic sequencing panels.SPG7 transcript level quantification was performed from whole blood RNA on a digital droplet qPCR system. Results: We identified 4 patients with pathogenic variants or variants of unknown significance in SPG7. No AFG3L2 mutations were identified. We provide evidence for pathogenicity for three mutations that were not previously associated with SPG7-related disease, based on their occurrence in context of the correct phenotype, and the reduction of transcript levels measured with RT-qPCR.A curious association of the heterozygous p.Gly349Ser mutation in association with an ALS-like syndrome is reported. Conclusions:SPG7 mutations sequencing has high diagnostic yield in late onset paraparesis

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8

Atorino, Luigia, Laura Silvestri, Mirko Koppen, Laura Cassina, Andrea Ballabio, Roberto Marconi, Thomas Langer, and Giorgio Casari. "Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia." Journal of Cell Biology 163, no. 4 (November 17, 2003): 777–87. http://dx.doi.org/10.1083/jcb.200304112.

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Mmutations in paraplegin, a putative mitochondrial metallopeptidase of the AAA family, cause an autosomal recessive form of hereditary spastic paraplegia (HSP). Here, we analyze the function of paraplegin at the cellular level and characterize the phenotypic defects of HSP patients' cells lacking this protein. We demonstrate that paraplegin coassembles with a homologous protein, AFG3L2, in the mitochondrial inner membrane. These two proteins form a high molecular mass complex, which we show to be aberrant in HSP fibroblasts. The loss of this complex causes a reduced complex I activity in mitochondria and an increased sensitivity to oxidant stress, which can both be rescued by exogenous expression of wild-type paraplegin. Furthermore, complementation studies in yeast demonstrate functional conservation of the human paraplegin–AFG3L2 complex with the yeast m-AAA protease and assign proteolytic activity to this structure. These results shed new light on the molecular pathogenesis of HSP and functionally link AFG3L2 to this neurodegenerative disease.

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9

Charif, Majida, Arnaud Chevrollier, Naïg Gueguen, Céline Bris, David Goudenège, Valérie Desquiret-Dumas, Stéphanie Leruez, et al. "Mutations in the m-AAA proteases AFG3L2 and SPG7 are causing isolated dominant optic atrophy." Neurology Genetics 6, no. 3 (May 20, 2020): e428. http://dx.doi.org/10.1212/nxg.0000000000000428.

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ObjectiveTo improve the genetic diagnosis of dominant optic atrophy (DOA), the most frequently inherited optic nerve disease, and infer genotype-phenotype correlations.MethodsExonic sequences of 22 genes were screened by new-generation sequencing in patients with DOA who were investigated for ophthalmology, neurology, and brain MRI.ResultsWe identified 7 and 8 new heterozygous pathogenic variants in SPG7 and AFG3L2. Both genes encode for mitochondrial matricial AAA (m-AAA) proteases, initially involved in recessive hereditary spastic paraplegia type 7 (HSP7) and dominant spinocerebellar ataxia 28 (SCA28), respectively. Notably, variants in AFG3L2 that result in DOA are located in different domains to those reported in SCA28, which likely explains the lack of clinical overlap between these 2 phenotypic manifestations. In comparison, the SPG7 variants identified in DOA are interspersed among those responsible for HSP7 in which optic neuropathy has previously been reported.ConclusionsOur results position SPG7 and AFG3L2 as candidate genes to be screened in DOA and indicate that regulation of mitochondrial protein homeostasis and maturation by m-AAA proteases are crucial for the maintenance of optic nerve physiology.

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10

Sacco, Tiziana, Enrica Boda, Eriola Hoxha, Riccardo Pizzo, Claudia Cagnoli, Alfredo Brusco, and Filippo Tempia. "Mouse brain expression patterns of Spg7, Afg3l1, and Afg3l2 transcripts, encoding for the mitochondrial m-AAA protease." BMC Neuroscience 11, no. 1 (2010): 55. http://dx.doi.org/10.1186/1471-2202-11-55.

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11

Richter, Uwe, Kah Ying Ng, Fumi Suomi, Paula Marttinen, Taina Turunen, Christopher Jackson, Anu Suomalainen, et al. "Mitochondrial stress response triggered by defects in protein synthesis quality control." Life Science Alliance 2, no. 1 (January 25, 2019): e201800219. http://dx.doi.org/10.26508/lsa.201800219.

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Mitochondria have a compartmentalized gene expression system dedicated to the synthesis of membrane proteins essential for oxidative phosphorylation. Responsive quality control mechanisms are needed to ensure that aberrant protein synthesis does not disrupt mitochondrial function. Pathogenic mutations that impede the function of the mitochondrial matrix quality control protease complex composed of AFG3L2 and paraplegin cause a multifaceted clinical syndrome. At the cell and molecular level, defects to this quality control complex are defined by impairment to mitochondrial form and function. Here, we establish the etiology of these phenotypes. We show how disruptions to the quality control of mitochondrial protein synthesis trigger a sequential stress response characterized first by OMA1 activation followed by loss of mitochondrial ribosomes and by remodelling of mitochondrial inner membrane ultrastructure. Inhibiting mitochondrial protein synthesis with chloramphenicol completely blocks this stress response. Together, our data establish a mechanism linking major cell biological phenotypes of AFG3L2 pathogenesis and show how modulation of mitochondrial protein synthesis can exert a beneficial effect on organelle homeostasis.

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Ding, Bojian, Dwight W. Martin, Anthony J. Rampello, and Steven E. Glynn. "Dissecting Substrate Specificities of the Mitochondrial AFG3L2 Protease." Biochemistry 57, no. 28 (June 22, 2018): 4225–35. http://dx.doi.org/10.1021/acs.biochem.8b00565.

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13

Bettegazzi, Barbara, Ilaria Pelizzoni, Floramarida Salerno Scarzella, Lisa Michelle Restelli, Daniele Zacchetti, Francesca Maltecca, Giorgio Casari, Fabio Grohovaz, and Franca Codazzi. "Upregulation of Peroxiredoxin 3 Protects Afg3l2-KO Cortical Neurons In Vitro from Oxidative Stress: A Paradigm for Neuronal Cell Survival under Neurodegenerative Conditions." Oxidative Medicine and Cellular Longevity 2019 (October 31, 2019): 1–13. http://dx.doi.org/10.1155/2019/4721950.

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Several neurodegenerative disorders exhibit selective vulnerability, with subsets of neurons more affected than others, possibly because of the high expression of an altered gene or the presence of particular features that make them more susceptible to insults. On the other hand, resilient neurons may display the ability to develop antioxidant defenses, particularly in diseases of mitochondrial origin, where oxidative stress might contribute to the neurodegenerative process. In this work, we investigated the oxidative stress response of embryonic fibroblasts and cortical neurons obtained from Afg3l2-KO mice. AFG3L2 encodes a subunit of a protease complex that is expressed in mitochondria and acts as both quality control and regulatory enzyme affecting respiration and mitochondrial dynamics. When cells were subjected to an acute oxidative stress protocol, the survival of AFG3L2-KO MEFs was not significantly influenced and was comparable to that of WT; however, the basal level of the antioxidant molecule glutathione was higher. Indeed, glutathione depletion strongly affected the viability of KO, but not of WT MEF, thereby indicating that oxidative stress is more elevated in KO MEF even though well controlled by glutathione. On the other hand, when cortical KO neurons were put in culture, they immediately appeared more vulnerable than WT to the acute oxidative stress condition, but after few days in vitro, the situation was reversed with KO neurons being more resistant than WT to acute stress. This compensatory, protective competence was not due to the upregulation of glutathione, rather of two mitochondrial antioxidant proteins: superoxide dismutase 2 and, at an even higher level, peroxiredoxin 3. This body of evidence sheds light on the capability of neurons to activate neuroprotective pathways and points the attention to peroxiredoxin 3, an antioxidant enzyme that might be critical for neuronal survival also in other disorders affecting mitochondria.

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Almajan, Eva R., Ricarda Richter, Lars Paeger, Paola Martinelli, Esther Barth, Thorsten Decker, Nils-Göran Larsson, Peter Kloppenburg, Thomas Langer, and Elena I. Rugarli. "AFG3L2 supports mitochondrial protein synthesis and Purkinje cell survival." Journal of Clinical Investigation 122, no. 11 (October 8, 2012): 4048–58. http://dx.doi.org/10.1172/jci64604.

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15

Maltecca, F., A. Aghaie, D. G. Schroeder, L. Cassina, B. A. Taylor, S. J. Phillips, M. Malaguti, et al. "The Mitochondrial Protease AFG3L2 Is Essential for Axonal Development." Journal of Neuroscience 28, no. 11 (March 12, 2008): 2827–36. http://dx.doi.org/10.1523/jneurosci.4677-07.2008.

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16

Smets, K., T. Deconinck, J. Baets, A. Sieben, J. J. Martin, I. Smouts, S. Wang, et al. "Partial deletion of AFG3L2 causing spinocerebellar ataxia type 28." Neurology 82, no. 23 (May 9, 2014): 2092–100. http://dx.doi.org/10.1212/wnl.0000000000000491.

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17

Banfi, Sandro, Maria Teresa Bassi, Grazia Andolfi, Anna Marchitiello, Stefania Zanotta, Andrea Ballabio, Giorgio Casari, and Brunella Franco. "Identification and Characterization of AFG3L2, a Novel Paraplegin-Related Gene." Genomics 59, no. 1 (July 1999): 51–58. http://dx.doi.org/10.1006/geno.1999.5818.

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18

Joerg, H., J. Muntwyler, M. L. Glowatzki-Mullis, E. Ahrens, M. Asai-Coakwell, and G. Stranzinger. "Bovine spinal muscular atrophy: AFG3L2 is not a positional candidate gene." Journal of Animal Breeding and Genetics 122, s1 (April 2005): 103–7. http://dx.doi.org/10.1111/j.1439-0388.2005.00489.x.

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19

Caporali, Leonardo, Stefania Magri, Andrea Legati, Valentina Del Dotto, Francesca Tagliavini, Francesca Balistreri, Alessia Nasca, et al. "ATPase Domain AFG3L2 Mutations Alter OPA1 Processing and Cause Optic Neuropathy." Annals of Neurology 88, no. 1 (April 21, 2020): 18–32. http://dx.doi.org/10.1002/ana.25723.

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20

Chiang, Han-Lin, Jong-Ling Fuh, Yu-Shuen Tsai, Bing-Wen Soong, Yi-Chu Liao, and Yi-Chung Lee. "Expanding the phenotype of AFG3L2 mutations: Late-onset autosomal recessive spinocerebellar ataxia." Journal of the Neurological Sciences 428 (September 2021): 117600. http://dx.doi.org/10.1016/j.jns.2021.117600.

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21

Di Bella, Daniela, Federico Lazzaro, Alfredo Brusco, Massimo Plumari, Giorgio Battaglia, Annalisa Pastore, Adele Finardi, et al. "Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28." Nature Genetics 42, no. 4 (March 7, 2010): 313–21. http://dx.doi.org/10.1038/ng.544.

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22

Qu, Jane, Connie K. Wu, José Rafael P. Zuzuárregui, and Anna D. Hohler. "A novel AFG3L2 mutation in a Somalian patient with spinocerebellar ataxia type 28." Journal of the Neurological Sciences 358, no. 1-2 (November 2015): 530–31. http://dx.doi.org/10.1016/j.jns.2015.10.003.

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23

Szpisjak, Laszlo, Viola L. Nemeth, Noemi Szepfalusi, Denes Zadori, Zoltan Maroti, Tibor Kalmar, Laszlo Vecsei, and Peter Klivenyi. "Neurocognitive Characterization of an SCA28 Family Caused by a Novel AFG3L2 Gene Mutation." Cerebellum 16, no. 5-6 (June 28, 2017): 979–85. http://dx.doi.org/10.1007/s12311-017-0870-9.

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24

Maltecca, F., D. De Stefani, L. Cassina, F. Consolato, M. Wasilewski, L. Scorrano, R. Rizzuto, and G. Casari. "Respiratory dysfunction by AFG3L2 deficiency causes decreased mitochondrial calcium uptake via organellar network fragmentation." Human Molecular Genetics 21, no. 17 (June 7, 2012): 3858–70. http://dx.doi.org/10.1093/hmg/dds214.

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25

Eskandrani, Alaa, Amal AlHashem, El-Sayed Ali, Saad AlShahwan, Kalthoum Tlili, Khaled Hundallah, and Brahim Tabarki. "Recessive AFG3L2 Mutation Causes Progressive Microcephaly, Early Onset Seizures, Spasticity, and Basal Ganglia Involvement." Pediatric Neurology 71 (June 2017): 24–28. http://dx.doi.org/10.1016/j.pediatrneurol.2017.03.019.

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Musova, Zuzana, Michaela Kaiserova, Eva Kriegova, Regina Fillerova, Peter Vasovcak, Alena Santava, Katerina Mensikova, et al. "A Novel Frameshift Mutation in the AFG3L2 Gene in a Patient with Spinocerebellar Ataxia." Cerebellum 13, no. 3 (November 23, 2013): 331–37. http://dx.doi.org/10.1007/s12311-013-0538-z.

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Richter, Uwe, Taina Lahtinen, Paula Marttinen, Fumi Suomi, and Brendan J. Battersby. "Quality control of mitochondrial protein synthesis is required for membrane integrity and cell fitness." Journal of Cell Biology 211, no. 2 (October 26, 2015): 373–89. http://dx.doi.org/10.1083/jcb.201504062.

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Mitochondrial ribosomes synthesize a subset of hydrophobic proteins required for assembly of the oxidative phosphorylation complexes. This process requires temporal and spatial coordination and regulation, so quality control of mitochondrial protein synthesis is paramount to maintain proteostasis. We show how impaired turnover of de novo mitochondrial proteins leads to aberrant protein accumulation in the mitochondrial inner membrane. This creates a stress in the inner membrane that progressively dissipates the mitochondrial membrane potential, which in turn stalls mitochondrial protein synthesis and fragments the mitochondrial network. The mitochondrial m-AAA protease subunit AFG3L2 is critical to this surveillance mechanism that we propose acts as a sensor to couple the synthesis of mitochondrial proteins with organelle fitness, thus ensuring coordinated assembly of the oxidative phosphorylation complexes from two sets of ribosomes.

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Kondadi, A. K., S. Wang, S. Montagner, N. Kladt, A. Korwitz, P. Martinelli, D. Herholz, et al. "Loss of the m-AAA protease subunit AFG3L2 causes mitochondrial transport defects and tau hyperphosphorylation." EMBO Journal 33, no. 9 (March 28, 2014): 1011–26. http://dx.doi.org/10.1002/embj.201387009.

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29

Cagnoli, Claudia, Giovanni Stevanin, Alessandro Brussino, Marco Barberis, Cecilia Mancini, Russell L. Margolis, Susan E. Holmes, et al. "Missense mutations in the AFG3L2 proteolytic domain account for ∼1.5% of European autosomal dominant cerebellar ataxias." Human Mutation 31, no. 10 (September 7, 2010): 1117–24. http://dx.doi.org/10.1002/humu.21342.

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30

Tsai, Chen-Wei, Yujiao Wu, Ping-Chieh Pao, Charles B. Phillips, Carole Williams, Christopher Miller, Matthew Ranaghan, and Ming-Feng Tsai. "Proteolytic control of the mitochondrial calcium uniporter complex." Proceedings of the National Academy of Sciences 114, no. 17 (April 10, 2017): 4388–93. http://dx.doi.org/10.1073/pnas.1702938114.

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The mitochondrial calcium uniporter is a Ca2+-activated Ca2+ channel complex mediating mitochondrial Ca2+ uptake, a process crucial for Ca2+ signaling, bioenergetics, and cell death. The uniporter is composed of the pore-forming MCU protein, the gatekeeping MICU1 and MICU2 subunits, and EMRE, a single-pass membrane protein that links MCU and MICU1 together. As a bridging subunit required for channel function, EMRE could paradoxically inhibit uniporter complex formation if expressed in excess. Here, we show that mitochondrial mAAA proteases AFG3L2 and SPG7 rapidly degrade unassembled EMRE using the energy of ATP hydrolysis. Once EMRE is incorporated into the complex, its turnover is inhibited >15-fold. Protease-resistant EMRE mutants produce uniporter subcomplexes that induce constitutive Ca2+ leakage into mitochondria, a condition linked to debilitating neuromuscular disorders in humans. The results highlight the dynamic nature of uniporter subunit assembly, which must be tightly regulated to ensure proper mitochondrial responses to intracellular Ca2+ signals.

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Mancini, Cecilia, Eriola Hoxha, Luisa Iommarini, Alessandro Brussino, Uwe Richter, Francesca Montarolo, Claudia Cagnoli, et al. "Mice harbouring a SCA28 patient mutation in AFG3L2 develop late-onset ataxia associated with enhanced mitochondrial proteotoxicity." Neurobiology of Disease 124 (April 2019): 14–28. http://dx.doi.org/10.1016/j.nbd.2018.10.018.

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32

Almontashiri, Naif A. M., Hsiao-Huei Chen, Ryan J. Mailloux, Takashi Tatsuta, Allen C. T. Teng, Ahmad B. Mahmoud, Tiffany Ho, et al. "SPG7 Variant Escapes Phosphorylation-Regulated Processing by AFG3L2, Elevates Mitochondrial ROS, and Is Associated with Multiple Clinical Phenotypes." Cell Reports 7, no. 3 (May 2014): 834–47. http://dx.doi.org/10.1016/j.celrep.2014.03.051.

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Maltecca, F., R. Magnoni, F. Cerri, G. A. Cox, A. Quattrini, and G. Casari. "Haploinsufficiency of AFG3L2, the Gene Responsible for Spinocerebellar Ataxia Type 28, Causes Mitochondria-Mediated Purkinje Cell Dark Degeneration." Journal of Neuroscience 29, no. 29 (July 22, 2009): 9244–54. http://dx.doi.org/10.1523/jneurosci.1532-09.2009.

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Löbbe, Anna Mareike, Jun-Suk Kang, Rüdiger Hilker, Holger Hackstein, Ulrich Müller, and Dagmar Nolte. "A Novel Missense Mutation in AFG3L2 Associated with Late Onset and Slow Progression of Spinocerebellar Ataxia Type 28." Journal of Molecular Neuroscience 52, no. 4 (November 29, 2013): 493–96. http://dx.doi.org/10.1007/s12031-013-0187-1.

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Pierson, Tyler Mark, David Adams, Florian Bonn, Paola Martinelli, Praveen F. Cherukuri, Jamie K. Teer, Nancy F. Hansen, et al. "Whole-Exome Sequencing Identifies Homozygous AFG3L2 Mutations in a Spastic Ataxia-Neuropathy Syndrome Linked to Mitochondrial m-AAA Proteases." PLoS Genetics 7, no. 10 (October 13, 2011): e1002325. http://dx.doi.org/10.1371/journal.pgen.1002325.

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Calandra, Cristian R., Guadalupe Buda, Sebastian A. Vishnopolska, Jaen Oliveri, Federico A. Olivieri, María I. Pérez Millán, German Biagioli, Luis A. Miquelini, Alejandro L. Pellene, and Marcelo A. Marti. "Spastic ataxia with eye-of-the-tiger-like sign in 4 siblings due to novel compound heterozygous AFG3L2 mutation." Parkinsonism & Related Disorders 73 (April 2020): 52–54. http://dx.doi.org/10.1016/j.parkreldis.2020.03.020.

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Puchades, Cristina, Bojian Ding, Albert Song, R. Luke Wiseman, Gabriel C. Lander, and Steven E. Glynn. "Unique Structural Features of the Mitochondrial AAA+ Protease AFG3L2 Reveal the Molecular Basis for Activity in Health and Disease." Molecular Cell 75, no. 5 (September 2019): 1073–85. http://dx.doi.org/10.1016/j.molcel.2019.06.016.

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Tunc, Sinem, Marija Dulovic-Mahlow, Hauke Baumann, Magdalena Khira Baaske, Magdalena Jahn, Johanna Junker, Alexander Münchau, Norbert Brüggemann, and Katja Lohmann. "Spinocerebellar Ataxia Type 28—Phenotypic and Molecular Characterization of a Family with Heterozygous and Compound-Heterozygous Mutations in AFG3L2." Cerebellum 18, no. 4 (May 20, 2019): 817–22. http://dx.doi.org/10.1007/s12311-019-01036-2.

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Pareek, Gautam, and Leo J. Pallanck. "Inactivation of the mitochondrial protease Afg3l2 results in severely diminished respiratory chain activity and widespread defects in mitochondrial gene expression." PLOS Genetics 16, no. 10 (October 19, 2020): e1009118. http://dx.doi.org/10.1371/journal.pgen.1009118.

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Magri, Stefania, Valentina Fracasso, Massimo Plumari, Enrico Alfei, Daniele Ghezzi, Cinzia Gellera, Paola Rusmini, et al. "Concurrent AFG3L2 and SPG7 mutations associated with syndromic parkinsonism and optic atrophy with aberrant OPA1 processing and mitochondrial network fragmentation." Human Mutation 39, no. 12 (October 10, 2018): 2060–71. http://dx.doi.org/10.1002/humu.23658.

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Svenstrup, Kirsten, Troels Tolstrup Nielsen, Frederik Aidt, Nina Rostgaard, Morten Duno, Flemming Wibrand, Tua Vinther-Jensen, et al. "SCA28: Novel Mutation in the AFG3L2 Proteolytic Domain Causes a Mild Cerebellar Syndrome with Selective Type-1 Muscle Fiber Atrophy." Cerebellum 16, no. 1 (February 11, 2016): 62–67. http://dx.doi.org/10.1007/s12311-016-0765-1.

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Škorja Milić, Nives, Klemen Dolinar, Katarina Miš, Urška Matkovič, Maruša Bizjak, Mojca Pavlin, Matej Podbregar, and Sergej Pirkmajer. "Suppression of Pyruvate Dehydrogenase Kinase by Dichloroacetate in Cancer and Skeletal Muscle Cells Is Isoform Specific and Partially Independent of HIF-1α." International Journal of Molecular Sciences 22, no. 16 (August 10, 2021): 8610. http://dx.doi.org/10.3390/ijms22168610.

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Abstract:

Inhibition of pyruvate dehydrogenase kinase (PDK) emerged as a potential strategy for treatment of cancer and metabolic disorders. Dichloroacetate (DCA), a prototypical PDK inhibitor, reduces the abundance of some PDK isoenzymes. However, the underlying mechanisms are not fully characterized and may differ across cell types. We determined that DCA reduced the abundance of PDK1 in breast (MDA-MB-231) and prostate (PC-3) cancer cells, while it suppressed both PDK1 and PDK2 in skeletal muscle cells (L6 myotubes). The DCA-induced PDK1 suppression was partially dependent on hypoxia-inducible factor-1α (HIF-1α), a transcriptional regulator of PDK1, in cancer cells but not in L6 myotubes. However, the DCA-induced alterations in the mRNA and the protein levels of PDK1 and/or PDK2 did not always occur in parallel, implicating a role for post-transcriptional mechanisms. DCA did not inhibit the mTOR signaling, while inhibitors of the proteasome or gene silencing of mitochondrial proteases CLPP and AFG3L2 did not prevent the DCA-induced reduction of the PDK1 protein levels. Collectively, our results suggest that DCA reduces the abundance of PDK in an isoform-dependent manner via transcriptional and post-transcriptional mechanisms. Differential response of PDK isoenzymes to DCA might be important for its pharmacological effects in different types of cells.

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Edener, Ulf, Janine Wöllner, Ute Hehr, Zacharias Kohl, Stefan Schilling, Friedmar Kreuz, Peter Bauer, Veronica Bernard, Gabriele Gillessen-Kaesbach, and Christine Zühlke. "Early onset and slow progression of SCA28, a rare dominant ataxia in a large four-generation family with a novel AFG3L2 mutation." European Journal of Human Genetics 18, no. 8 (March 31, 2010): 965–68. http://dx.doi.org/10.1038/ejhg.2010.40.

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Canafoglia, Laura, Silvana Franceschetti, Antonio Gambardella, Pasquale Striano, Anna Teresa Giallonardo, Paolo Tinuper, Carlo Di Bonaventura, et al. "Progressive Myoclonus Epilepsies." Neurology Genetics 7, no. 6 (November 12, 2021): e641. http://dx.doi.org/10.1212/nxg.0000000000000641.

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Background and ObjectivesTo assess the current diagnostic yield of genetic testing for the progressive myoclonus epilepsies (PMEs) of an Italian series described in 2014 where Unverricht-Lundborg and Lafora diseases accounted for ∼50% of the cohort.MethodsOf 47/165 unrelated patients with PME of indeterminate genetic origin, 38 underwent new molecular evaluations. Various next-generation sequencing (NGS) techniques were applied including gene panel analysis (n = 7) and/or whole-exome sequencing (WES) (WES singleton n = 29, WES trio n = 7, and WES sibling n = 4). In 1 family, homozygosity mapping was followed by targeted NGS. Clinically, the patients were grouped in 4 phenotypic categories: “Unverricht-Lundborg disease-like PME,” “late-onset PME,” “PME plus developmental delay,” and “PME plus dementia.”ResultsSixteen of 38 (42%) unrelated patients reached a positive diagnosis, increasing the overall proportion of solved families in the total series from 72% to 82%. Likely pathogenic variants were identified in NEU1 (2 families), CERS1 (1 family), and in 13 nonfamilial patients in KCNC1 (3), DHDDS (3), SACS, CACNA2D2, STUB1, AFG3L2, CLN6, NAXE, and CHD2. Across the different phenotypic categories, the diagnostic rate was similar, and the same gene could be found in different phenotypic categories.DiscussionThe application of NGS technology to unsolved patients with PME has revealed a collection of very rare genetic causes. Pathogenic variants were detected in both established PME genes and in genes not previously associated with PME, but with progressive ataxia or with developmental encephalopathies. With a diagnostic yield >80%, PME is one of the best genetically defined epilepsy syndromes.

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Baviera-Muñoz, Raquel, Lidón Carretero-Vilarroig, Juan Francisco Vázquez-Costa, Carlos Morata-Martínez, Marina Campins-Romeu, Nuria Muelas, Isabel Sastre-Bataller, et al. "Diagnostic Efficacy of Genetic Studies in a Series of Hereditary Cerebellar Ataxias in Eastern Spain." Neurology Genetics 8, no. 6 (November 14, 2022): e200038. http://dx.doi.org/10.1212/nxg.0000000000200038.

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Background and ObjectivesTo determine the diagnostic efficacy of clinical exome-targeted sequencing (CES) and spinocerebellar ataxia 36 (SCA36) screening in a real-life cohort of patients with cerebellar ataxia (CA) from Eastern Spain.MethodsA total of 130 unrelated patients with CA, negative for common trinucleotide repeat expansions (SCA1, SCA2, SCA3, SCA6, SCA7, SCA8, SCA12, SCA17, dentatorubral pallidoluysian atrophy [DRPLA], and Friedreich ataxia), were studied with CES. Bioinformatic and genotype-phenotype analyses were performed to assess the pathogenicity of the variants encountered. Copy number variants were analyzed when appropriate. In undiagnosed dominant and sporadic cases, repeat primed PCR was used to screen for the presence of a repeat expansion in theNOP56gene.ResultsCES identified pathogenic or likely pathogenic variants in 50 families (39%), including 23 novel variants. Overall, there was a high genetic heterogeneity, and the most frequent genetic diagnosis wasSPG7(n = 15), followed bySETX(n = 6),CACNA1A(n = 5),POLR3A(n = 4), andSYNE1(n = 3). In addition, 17 families displayed likely pathogenic/pathogenic variants in 14 different genes:KCND3(n = 2),KIF1C(n = 2),CYP27A1A(n = 2),AFG3L2(n = 1),ANO10(n = 1),CAPN1(n = 1),CWF19L1(n = 1),ITPR1(n = 1),KCNA1(n = 1),OPA1(n = 1),PNPLA6(n = 1),SPG11(n = 1),SPTBN2(n = 1), andTPP1(n = 1). Twenty-two novel variants were characterized. SCA36 was diagnosed in 11 families, all with autosomal dominant (AD) presentation. SCA36 screening increased the total diagnostic rate to 47% (n = 61/130). Ultimately, undiagnosed patients showed delayed age at onset (p< 0.05) and were more frequently sporadic.DiscussionOur study provides insight into the genetic landscape of CA in Eastern Spain. Although CES was an effective approach to capture genetic heterogeneity, most patients remained undiagnosed. SCA36 was found to be a relatively frequent form and, therefore, should be tested prior to CES in familial AD presentations in particular geographical regions.

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lv, Yue, Chun-hui Yuan, Lu-yao Han, Gao-ru Huang, Ling-ce Ju, Ling-hui Chen, Hai-ying Han, Chong Zhang, and Ling-hui Zeng. "The Overexpression of SLC25A13 Predicts Poor Prognosis and Is Correlated with Immune Cell Infiltration in Patients with Skin Cutaneous Melanoma." Disease Markers 2022 (May 14, 2022): 1–15. http://dx.doi.org/10.1155/2022/4091978.

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Purpose. Skin cutaneous melanoma (SKCM) is one of the most malignant and aggressive cancers with poor prognosis due to its rapid progression towards metastasis. Thus, finding clinically relevant biomarkers for early diagnosis, prognosis, and therapy prediction is essential. This study focused on the identification of SLC25A13 as a novel biomarker for SKCM and is aimed at investigating the biological functions of solute carrier family 25 member 13 (SLC25A13) in the development of SKCM. Methods. GEPIA was used to analyze the diagnostic and prognostic values of SLC25A13 in SKCM using the TCGA dataset. PrognoScan was used to validate the prognostic value of SLC25A13 and its coexpressed genes in SKCM. TISIDB was established to reveal the relationship between the expression of SLC25A13 and immune infiltration in SKCM. The protein expression of SLC25A13 in SKCM was evaluated by the Human Protein Atlas. The signaling pathways and biological functions of SLC25A13 in SKCM were analyzed by LinkOmics. Metascape was applied to analyze the functional enrichment analysis of SLC25A13. Protein-protein interaction analysis of SLC25A13 was performed by GeneMANIA. Results. The mRNA and protein levels of SLC25A13 in the SKCM were much higher than those in the normal tissue. Furthermore, the overexpression of SLC25A13 predicts worse outcomes of SKCM patients. Moreover, the SLC25A13 expression was negatively correlated with the immune infiltration level of SKCM. The overexpression of SLC25A13 coexpressed genes, such as ACLY and AFG3L2, and SCL25A13 interacting genes also predicted the unfavorable prognosis of SKCM patients. Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis of SLC25A13 coexpressed genes showed that these genes are enriched in ATPase activity, cell cycle, mTOR, and VEGFA-VEGFR2 signaling pathways, which were relevant to tumor development and angiogenesis. Gene set enrichment analysis (GSEA) demonstrated that the SLC25A13 expression was related to infiltrating immune cells in SKCM. Conclusion. Our findings revealed that SLC25A13 might be a potential prognostic and therapeutic biomarker for SKCM.

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Newton, J. L., R. A. Kenny, R. Frearson, and R. M. Francis. "A prospective evaluation of bone mineral density measurement in females who have fallen." Age and Ageing 32, no. 5 (September 1, 2003): 497–502. http://dx.doi.org/10.1093/ageing/afg062.

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Hwang, H. F., W. M. Liang, Y. N. Chiu, and M. R. Lin. "Suitability of the WHOQOL-BREF for community-dwelling older people in Taiwan." Age and Ageing 32, no. 6 (November 1, 2003): 593–600. http://dx.doi.org/10.1093/ageing/afg102.

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Starr, J. M., H. Martin, J. McCoubrey, G. Gibson, and I. R. Poxton. "Risk factors for Clostridium difficile colonisation and toxin production." Age and Ageing 32, no. 6 (November 1, 2003): 657–60. http://dx.doi.org/10.1093/ageing/afg112.

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Conroy, Simon, Sophie Moulias, and Wassif S. Wassif. "Primary hyperparathyroidism in the older person." Age and Ageing 32, no. 6 (November 2003): 571–78. http://dx.doi.org/10.1093/ageing/afg122.

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