E3 ubiquitin ligase Hades negatively regulates the exonuclear function of p53

Jung, Jin Hyuk; Bae, Seunghee; Lee, J. Y.; Woo, Seon Rang; J., H.; Yoon, Younju; Suh, Kyung‐Suk; Lee, S. J.; Park, I. C.; Jin, Yetao; Lee, K. H.; An, Shi; Lee, J. H.

doi:10.1038/cdd.2011.57

Cited by 48 publications

(39 citation statements)

References 34 publications

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“…-Ultrastructural analysis is important to directly visualize MDVs within the cell using immunogold labeling. We identified MAPL as a SUMO E3 ligase containing two transmembrane domains, with a C-terminal RING domain exposed to the cytosol and a approximately 40 kDa intermembrane space domain of unknown function Neuspiel et al, 2008;Zhang et al, 2008;Braschi et al, 2009;Jung et al, 2011). The probabilities of capturing an unbudded MDV from the mitochondria is low unless cells are treated with stress agents like xanthine oxidaze/xanthine.…”

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confidence: 99%

“…Most of these tail-anchored proteins appear to be imported into peroxisomes using the canonical, peroxisomal import machinery (Delille & Schrader, 2008). We identified MAPL as a SUMO E3 ligase containing two transmembrane domains, with a C-terminal RING domain exposed to the cytosol and a approximately 40 kDa intermembrane space domain of unknown function Neuspiel et al, 2008;Zhang et al, 2008;Braschi et al, 2009;Jung et al, 2011). This protein has a unique evolutionary phylogeny, with the intermembrane space and transmembrane domains being conserved within distant bacteria, as well as plants (Andrade-Navarro et al, 2009).…”

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confidence: 99%

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A new pathway for mitochondrial quality control: mitochondrial‐derived vesicles

et al. 2014

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The last decade has been marked by tremendous progress in our understanding of the cell biology of mitochondria, with the identification of molecules and mechanisms that regulate their fusion, fission, motility, and the architectural transitions within the inner membrane. More importantly, the manipulation of these machineries in tissues has provided links between mitochondrial dynamics and physiology. Indeed, just as the proteins required for fusion and fission were identified, they were quickly linked to both rare and common human diseases. This highlighted the critical importance of this emerging field to medicine, with new hopes of finding drugable targets for numerous pathologies, from neurodegenerative diseases to inflammation and cancer. In the midst of these exciting new discoveries, an unexpected new aspect of mitochondrial cell biology has been uncovered; the generation of small vesicular carriers that transport mitochondrial proteins and lipids to other intracellular organelles. These mitochondrial-derived vesicles (MDVs) were first found to transport a mitochondrial outer membrane protein MAPL to a subpopulation of peroxisomes. However, other MDVs did not target peroxisomes and instead fused with the late endosome, or multivesicular body. The Parkinson's disease-associated proteins Vps35, Parkin, and PINK1 are involved in the biogenesis of a subset of these MDVs, linking this novel trafficking pathway to human disease. In this review, we outline what has been learned about the mechanisms and functional importance of MDV transport and speculate on the greater impact of these pathways in cellular physiology.

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A new pathway for mitochondrial quality control: mitochondrial‐derived vesicles

et al. 2014

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“…It is not uncommon for an E3 ubiquitin ligase to be multifunctional and have different substrates. For example, MAPL itself has several known substrate proteins in different physiological processes, including the mitochondrial and peroxisomal fission factor dynaminrelated protein DRP1 (Braschi et al, 2009), E3 ubiquitin ligase TRAF2 in mitochondrial hyperfusion (Zemirli et al, 2014), ULK1 in mitophagy (Li et al, 2015), mitofusin in mitochondrial integrity maintenance (Yun et al, 2014), RIG-I in mitochondrial antiviral response (Jenkins et al, 2013), the Ser/Thr kinase Akt in cell proliferation and viability (Bae et al, 2012), and p53 and p73 when they translocate to mitochondria under cell stress (Jung et al, 2011;Min et al, 2015). When we performed a phylogenetic analysis using SP1, its two homologs from Arabidopsis SPL1 and SPL2, and homologous sequences from other eukaryotic species, MAPL was grouped together with SP1 and SPL1 in the same subclade conserved in plants and animals, whereas SPL2 belonged to a plant-specific subclade, suggesting a strong evolutionary relationship between SP1 and MAPL (Pan et al, 2016).…”

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The Arabidopsis E3 Ubiquitin Ligase SP1 Targets to Chloroplasts, Peroxisomes, and Mitochondria

Pan

2018

Plant Physiol.

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“…The mammalian protein most closely related to SP1 and SPL1 is the human MAPL (mitochondrial‐anchored protein ligase) protein, which is also named MULAN, MUL1, GIDE or HADES, and has diverse substrates involved in various processes, including mitochondrial fission, hyperfusion, and integrity maintenance, mitophagy, antiviral response, cell proliferation and cell stress response (Braschi et al ., ; Jung et al ., ; Bae et al ., ; Jenkins et al ., ; Yun et al ., ; Zemirli et al ., ; Li et al ., ; Min et al ., ). MAPL is associated with both mitochondria and a subpopulation of peroxisomes, but its function in the peroxisome is still unclear (Neuspiel et al ., ).…”

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confidence: 99%

The E3 ubiquitin ligase SP1‐like 1 plays a positive role in peroxisome biogenesis in Arabidopsis

et al. 2018

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Peroxisomes are dynamic organelles crucial for a variety of metabolic processes during the development of eukaryotic organisms, and are functionally linked to other subcellular organelles, such as mitochondria and chloroplasts. Peroxisomal matrix proteins are imported by peroxins (PEX proteins), yet the modulation of peroxin functions is poorly understood. We previously reported that, besides its known function in chloroplast protein import, the Arabidopsis E3 ubiquitin ligase SP1 (suppressor of ppi1 locus1) also targets to peroxisomes and mitochondria, and promotes the destabilization of the peroxisomal receptor-cargo docking complex components PEX13 and PEX14. Here we present evidence that in Arabidopsis, SP1's closest homolog SP1-like 1 (SPL1) plays an opposite role to SP1 in peroxisomes. In contrast to sp1, loss-of-function of SPL1 led to reduced peroxisomal β-oxidation activity, and enhanced the physiological and growth defects of pex14 and pex13 mutants. Transient co-expression of SPL1 and SP1 promoted each other's destabilization. SPL1 reduced the ability of SP1 to induce PEX13 turnover, and it is the N-terminus of SP1 and SPL1 that determines whether the protein is able to promote PEX13 turnover. Finally, SPL1 showed prevalent targeting to mitochondria, but rather weak and partial localization to peroxisomes. Our data suggest that these two members of the same E3 protein family utilize distinct mechanisms to modulate peroxisome biogenesis, where SPL1 reduces the function of SP1. Plants and possibly other higher eukaryotes may employ this small family of E3 enzymes to differentially modulate the dynamics of several organelles essential to energy metabolism via the ubiquitin-proteasome system.

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E3 ubiquitin ligase Hades negatively regulates the exonuclear function of p53

Cited by 48 publications

References 34 publications

A new pathway for mitochondrial quality control: mitochondrial‐derived vesicles

A new pathway for mitochondrial quality control: mitochondrial‐derived vesicles

The Arabidopsis E3 Ubiquitin Ligase SP1 Targets to Chloroplasts, Peroxisomes, and Mitochondria

The E3 ubiquitin ligase SP1‐like 1 plays a positive role in peroxisome biogenesis in Arabidopsis

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