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Journal articles on the topic 'AFG3L1P'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 February 2022

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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 (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 (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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3

Ehses, Sarah, Ines Raschke, Giuseppe Mancuso, et al. "Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1." Journal of Cell Biology 187, no. 7 (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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4

Duvezin-Caubet, Stéphane, Mirko Koppen, Johannes Wagener, 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 (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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5

Sacco, Tiziana, Enrica Boda, Eriola Hoxha, et al. "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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6

Tulli, Susanna, Andrea Del Bondio, Valentina Baderna, 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 (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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7

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 (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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8

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 (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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9

Atorino, Luigia, Laura Silvestri, Mirko Koppen, et al. "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 (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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10

Charif, Majida, Arnaud Chevrollier, Naïg Gueguen, et al. "Mutations in the m-AAA proteases AFG3L2 and SPG7 are causing isolated dominant optic atrophy." Neurology Genetics 6, no. 3 (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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11

Richter, Uwe, Kah Ying Ng, Fumi Suomi, et al. "Mitochondrial stress response triggered by defects in protein synthesis quality control." Life Science Alliance 2, no. 1 (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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12

Bettegazzi, Barbara, Ilaria Pelizzoni, Floramarida Salerno Scarzella, et al. "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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13

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

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14

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

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15

Almajan, Eva R., Ricarda Richter, Lars Paeger, et al. "AFG3L2 supports mitochondrial protein synthesis and Purkinje cell survival." Journal of Clinical Investigation 122, no. 11 (2012): 4048–58. http://dx.doi.org/10.1172/jci64604.

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16

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

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17

Banfi, Sandro, Maria Teresa Bassi, Grazia Andolfi, et al. "Identification and Characterization of AFG3L2, a Novel Paraplegin-Related Gene." Genomics 59, no. 1 (1999): 51–58. http://dx.doi.org/10.1006/geno.1999.5818.

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18

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

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19

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 (2005): 103–7. http://dx.doi.org/10.1111/j.1439-0388.2005.00489.x.

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20

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

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21

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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22

Shah, Zahid H., Vanessa Migliosi, Steven C. M. Miller, Aihui Wang, Thomas B. Friedman, and Howard T. Jacobs. "Chromosomal Locations of Three Human Nuclear Genes (RPSM12, TUFM, and AFG3L1) Specifying Putative Components of the Mitochondrial Gene Expression Apparatus." Genomics 48, no. 3 (1998): 384–88. http://dx.doi.org/10.1006/geno.1997.5166.

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23

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 (2015): 530–31. http://dx.doi.org/10.1016/j.jns.2015.10.003.

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24

Szpisjak, Laszlo, Viola L. Nemeth, Noemi Szepfalusi, et al. "Neurocognitive Characterization of an SCA28 Family Caused by a Novel AFG3L2 Gene Mutation." Cerebellum 16, no. 5-6 (2017): 979–85. http://dx.doi.org/10.1007/s12311-017-0870-9.

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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 (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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Eskandrani, Alaa, Amal AlHashem, El-Sayed Ali, et al. "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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27

Maltecca, F., D. De Stefani, L. Cassina, et al. "Respiratory dysfunction by AFG3L2 deficiency causes decreased mitochondrial calcium uptake via organellar network fragmentation." Human Molecular Genetics 21, no. 17 (2012): 3858–70. http://dx.doi.org/10.1093/hmg/dds214.

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28

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

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Kremmidiotis, Gabriel, Alison E. Gardner, Chatri Settasatian, Anna Savoia, Grant R. Sutherland, and David F. Callen. "Molecular and Functional Analyses of the Human and Mouse Genes Encoding AFG3L1, a Mitochondrial Metalloprotease Homologous to the Human Spastic Paraplegia Protein." Genomics 76, no. 1-3 (2001): 58–65. http://dx.doi.org/10.1006/geno.2001.6560.

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30

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

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Tsai, Chen-Wei, Yujiao Wu, Ping-Chieh Pao, et al. "Proteolytic control of the mitochondrial calcium uniporter complex." Proceedings of the National Academy of Sciences 114, no. 17 (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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Cagnoli, Claudia, Giovanni Stevanin, Alessandro Brussino, et al. "Missense mutations in the AFG3L2 proteolytic domain account for ∼1.5% of European autosomal dominant cerebellar ataxias." Human Mutation 31, no. 10 (2010): 1117–24. http://dx.doi.org/10.1002/humu.21342.

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33

Mancini, Cecilia, Eriola Hoxha, Luisa Iommarini, 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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34

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 (2009): 9244–54. http://dx.doi.org/10.1523/jneurosci.1532-09.2009.

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35

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 (2013): 493–96. http://dx.doi.org/10.1007/s12031-013-0187-1.

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36

Almontashiri, Naif A. M., Hsiao-Huei Chen, Ryan J. Mailloux, 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 (2014): 834–47. http://dx.doi.org/10.1016/j.celrep.2014.03.051.

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Škorja Milić, Nives, Klemen Dolinar, Katarina Miš та ін. "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, № 16 (2021): 8610. http://dx.doi.org/10.3390/ijms22168610.

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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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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 (2019): 1073–85. http://dx.doi.org/10.1016/j.molcel.2019.06.016.

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Calandra, Cristian R., Guadalupe Buda, Sebastian A. Vishnopolska, et al. "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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Pierson, Tyler Mark, David Adams, Florian Bonn, 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 (2011): e1002325. http://dx.doi.org/10.1371/journal.pgen.1002325.

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Tunc, Sinem, Marija Dulovic-Mahlow, Hauke Baumann, et al. "Spinocerebellar Ataxia Type 28—Phenotypic and Molecular Characterization of a Family with Heterozygous and Compound-Heterozygous Mutations in AFG3L2." Cerebellum 18, no. 4 (2019): 817–22. http://dx.doi.org/10.1007/s12311-019-01036-2.

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Broadley, Sarah A., Christina M. Demlow, and Thomas D. Fox. "Peripheral Mitochondrial Inner Membrane Protein, Mss2p, Required for Export of the Mitochondrially Coded Cox2p C Tail inSaccharomyces cerevisiae." Molecular and Cellular Biology 21, no. 22 (2001): 7663–72. http://dx.doi.org/10.1128/mcb.21.22.7663-7672.2001.

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ABSTRACT Cytochrome oxidase subunit 2 (Cox2p) is synthesized on the matrix side of the mitochondrial inner membrane, and its N- and C-terminal domains are exported across the inner membrane by distinct mechanisms. The Saccharomyces cerevisiaenuclear gene MSS2 was previously shown to be necessary for Cox2p accumulation. We have used pulse-labeling studies and the expression of the ARG8 m reporter at the COX2 locus in an mss2 mutant to demonstrate that Mss2p is not required for Cox2p synthesis but rather for its accumulation. Mutational inactivation of the proteolytic function of the matrix-localized Yta10p (Afg3p) AAA-protease partially stabilizes Cox2p in an mss2 mutant but does not restore assembly of cytochrome oxidase. In the absence of Mss2p, the Cox2p N terminus is exported, but Cox2p C-terminal export and assembly of Cox2p into cytochrome oxidase is blocked. Epitope-tagged Mss2p is tightly, but peripherally, associated with the inner membrane and protected by it from externally added proteases. Taken together, these data indicate that Mss2p plays a role in recognizing the Cox2p C tail in the matrix and promoting its export.

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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 (2020): e1009118. http://dx.doi.org/10.1371/journal.pgen.1009118.

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Svenstrup, Kirsten, Troels Tolstrup Nielsen, Frederik Aidt, 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 (2016): 62–67. http://dx.doi.org/10.1007/s12311-016-0765-1.

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Magri, Stefania, Valentina Fracasso, Massimo Plumari, 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 (2018): 2060–71. http://dx.doi.org/10.1002/humu.23658.

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Edener, Ulf, Janine Wöllner, Ute Hehr, et al. "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 (2010): 965–68. http://dx.doi.org/10.1038/ejhg.2010.40.

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Steglich, Gregor, Walter Neupert, and Thomas Langer. "Prohibitins Regulate Membrane Protein Degradation by the m-AAA Protease in Mitochondria." Molecular and Cellular Biology 19, no. 5 (1999): 3435–42. http://dx.doi.org/10.1128/mcb.19.5.3435.

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ABSTRACT Prohibitins comprise a protein family in eukaryotic cells with potential roles in senescence and tumor suppression. Phb1p and Phb2p, members of the prohibitin family in Saccharomyces cerevisiae, have been implicated in the regulation of the replicative life span of the cells and in the maintenance of mitochondrial morphology. The functional activities of these proteins, however, have not been elucidated. We demonstrate here that prohibitins regulate the turnover of membrane proteins by the m-AAA protease, a conserved ATP-dependent protease in the inner membrane of mitochondria. The m-AAA protease is composed of the homologous subunits Yta10p (Afg3p) and Yta12p (Rca1p). Deletion ofPHB1 or PHB2 impairs growth of Δyta10 or Δyta12 cells but does not affect cell growth in the presence of the m-AAA protease. A prohibitin complex with a native molecular mass of approximately 2 MDa containing Phb1p and Phb2p forms a supercomplex with them-AAA protease. Proteolysis of nonassembled inner membrane proteins by the m-AAA protease is accelerated in mitochondria lacking Phb1p or Phb2p, indicating a negative regulatory effect of prohibitins on m-AAA protease activity. These results functionally link members of two conserved protein families in eukaryotes to the degradation of membrane proteins in mitochondria.

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Guélin, Emmanuel, Martijn Rep, and Leslie A. Grivell. "Afg3p, a mitochondrial ATP-dependent metalloprotease, is involved in degradation of mitochondrially-encoded Cox1, Cox3, Cob, Su6, Su8 and Su9 subunits of the inner membrane complexes III, IV and V." FEBS Letters 381, no. 1-2 (1996): 42–46. http://dx.doi.org/10.1016/0014-5793(96)00074-9.

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Mancini, Cecilia, Laura Orsi, Yiran Guo, et al. "An atypical form of AOA2 with myoclonus associated with mutations in SETX and AFG3L2." BMC Medical Genetics 16, no. 1 (2015). http://dx.doi.org/10.1186/s12881-015-0159-0.

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Fracasso, Valentina, Federico Lazzaro, and Marco Muzi-Falconi. "Co-immunoprecipitation of human mitochondrial proteases AFG3L2 and paraplegin heterologously expressed in yeast cells." Protocol Exchange, March 7, 2010. http://dx.doi.org/10.1038/nprot.2010.26.

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