Pli1PIAS1 SUMO Ligase Protected by the Nuclear Pore-associated SUMO Protease Ulp1SENP1/2

Nie, Minghua; Boddy, Michael N.

doi:10.1074/jbc.m115.673038

Cited by 28 publications

(52 citation statements)

References 62 publications

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“…6). It is somewhat counter-intuitive that a SUMO protease promotes SUMO modification of 53BP1, but similar observations have been made in fission yeast, where the deletion of Nup132, the Schizosaccharomyces pombe homologue of human Nup133, caused delocalisation of Ulp1 from NPCs, leading to DNA damage and cell cycle defects (Nie and Boddy, 2015). These defects were thought to arise from inappropriate desumoylation of nucleoplasmic targets that are normally spatially protected from Ulp1.…”

Section: Discussion Silencing Nup153 Compromises Sumo1 Modification Omentioning

confidence: 85%

“…These defects were thought to arise from inappropriate desumoylation of nucleoplasmic targets that are normally spatially protected from Ulp1. Delocalised Ulp1 allowed an accumulation of SUMO chains on Pli1, a PIAS family SUMO E3 ligase and the S. pombe homologue of PIAS1, and its targeting for proteosomal degradation, which resulted in profound SUMO pathway and cell cycle defects (Nie and Boddy, 2015). It will be interesting to see whether a similar crosstalk between sumoylation and ubiquitylation of a PIAS family or another SUMO E3 ligase contributes to the defects in DDR seen in Nup153-depleted cells.…”

Section: Discussion Silencing Nup153 Compromises Sumo1 Modification Omentioning

confidence: 99%

“…No interaction of SENP2 with Tpr has been found , but SENP2 expression was reduced in HeLa cells depleted for Tpr (David-Watine, 2011). Delocalisation of Ulp1 from NPCs causes DNA damage and cell cycle defects, phenotypes attributed to inappropriate desumoylation of nucleoplasmic target proteins that are normally protected from Ulp1 (Nie and Boddy, 2015;Palancade et al, 2007;Zhang et al, 2002). Similarly, it has been shown that a mutant form of SENP2 that is unable to interact with Nup153 more effectively promotes desumoylation (Hang and Dasso, 2002), indicating that NPCs in fact play important roles in spatially restricting the activity of SUMO protease.…”

Section: Introductionmentioning

confidence: 99%

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Localisation of Nup153 and SENP1 to nuclear pore complexes is required for 53BP1-mediated DNA double-strand break repair

Duhéron

Nilles

Pecenko

et al. 2017

Journal of Cell Science

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The nuclear basket of nuclear pore complexes (NPCs) is composed of three nucleoporins: Nup153, Nup50 and Tpr. Nup153 has a role in DNA double-strand break (DSB) repair by promoting nuclear import of 53BP1 (also known as TP53BP1), a mediator of the DNA damage response. Here, we provide evidence that loss of Nup153 compromises 53BP1 sumoylation, a prerequisite for efficient accumulation of 53BP1 at DSBs. Depletion of Nup153 resulted in reduced SUMO1 modification of 53BP1 and the displacement of the SUMO protease SENP1 from NPCs. Artificial tethering of SENP1 to NPCs restored non-homologous end joining (NHEJ) in the absence of Nup153 and re-established 53BP1 sumoylation. Furthermore, Nup50 and Tpr, the two other nuclear basket nucleoporins, also contribute to proper DSB repair, in a manner distinct from Nup153. Similar to the role of Nup153, Tpr is implicated in NHEJ and homologous recombination (HR), whereas loss of Nup50 only affects NHEJ. Despite the requirement of all three nucleoporins for accurate NHEJ, only Nup153 is needed for proper nuclear import of 53BP1 and SENP1-dependent sumoylation of 53BP1. Our data support the role of Nup153 as an important regulator of 53BP1 activity and efficient NHEJ.

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Section: Discussion Silencing Nup153 Compromises Sumo1 Modification Omentioning

confidence: 85%

Section: Discussion Silencing Nup153 Compromises Sumo1 Modification Omentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Localisation of Nup153 and SENP1 to nuclear pore complexes is required for 53BP1-mediated DNA double-strand break repair

Duhéron

Nilles

Pecenko

et al. 2017

Journal of Cell Science

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“…STUbLs target both SUMO pathway enzymes and distinct groups of substrates (Fig 2A). For example, the yeast STUbLs can target Siz SUMO E3s; similarly a human STUbL, RNF4, targets SUMO E2 and multiple PIAS E3s that are heavily sumoylated (Kumar et al, 2017; Nie and Boddy, 2015; Westerbeck et al, 2014). In addition, RNF4 and another STUbL, Arkadia, affects the PML proteins.…”

Section: Global Changes In Sumoylation Levelsmentioning

confidence: 99%

SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes

Zhao

2018

Molecular Cell

196

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Summary Since the discovery of SUMO twenty years ago, SUMO conjugation has become a widely-recognized post-translational modification that targets a myriad of proteins in many processes. Great progress has been made in understanding the SUMO pathway enzymes, substrate sumoylation, and the interplay between sumoylation and other regulatory mechanisms in a variety of contexts. As these research directions continue to generate insights into SUMO-based regulation, several mechanisms by which sumoylation and desumoylation can orchestrate large biological effects are emerging. These include the ability to target multiple proteins within the same cellular structure or process, respond dynamically to external and internal stimuli, and modulate signaling pathways involving other post-translational modifications. Focusing on nuclear function and intracellular signaling, this review highlights a broad spectrum of historical data and recent advances with the aim of providing an overview of mechanisms underlying SUMO-mediated global effects to stimulate further inquiry into intriguing roles of SUMO.

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“…NPC also provides a platform for protein modification processes by the small ubiquitin‐like modifier (SUMO). One of the SUMO proteases, Ulp1, which removes a SUMO from SUMO‐conjugated proteins, localizes to the NE by interacting with a nucleoporin Nup132 (Nie and Boddy, ). Some SUMO‐conjugated proteins are targeted for degradation by a SUMO‐targeted ubiquitin ligase (STUbL).…”

Section: Organization Of Chromatin At the Nuclear Peripherymentioning

confidence: 99%

Spatial organization of theSchizosaccharomyces pombegenome within the nucleus

Matsuda

Asakawa

Haraguchi

et al. 2016

Yeast

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The fission yeast Schizosaccharomyces pombe is a useful experimental system for studying the organization of chromosomes within the cell nucleus. S. pombe has a small genome that is organized into three chromosomes. The small size of the genome and the small number of chromosomes are advantageous for cytological and genomewide studies of chromosomes; however, the small size of the nucleus impedes microscopic observations owing to limits in spatial resolution during imaging. Recent advances in microscopy, such as super-resolution microscopy, have greatly expanded the use of S. pombe as a model organism in a wide range of studies. In addition, biochemical studies, such as chromatin immunoprecipitation and chromosome conformation capture, have provided complementary approaches. Here, we review the spatial organization of the S. pombe genome as determined by a combination of cytological and biochemical studies.

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Pli1PIAS1 SUMO Ligase Protected by the Nuclear Pore-associated SUMO Protease Ulp1SENP1/2

Cited by 28 publications

References 62 publications

Localisation of Nup153 and SENP1 to nuclear pore complexes is required for 53BP1-mediated DNA double-strand break repair

Localisation of Nup153 and SENP1 to nuclear pore complexes is required for 53BP1-mediated DNA double-strand break repair

SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes

Spatial organization of theSchizosaccharomyces pombegenome within the nucleus

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