Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin.

Okura, Takafumi; Gong, Limin; Kamitani, Tetsu; Wada, Tomohiro; Okura, Izumi; Wei, Chik Fong; Chang, Hui-Ming; Yeh, Edward T.H.

doi:10.4049/jimmunol.157.10.4277

Cited by 287 publications

(9 citation statements)

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“…Several Fas-associated proteins have been reported in the literature (7)(8)(9)(10)(11)(12)(13)(14)(15)(16). These proteins were initially identified in a yeast-two hybrid system using the Fas cytoplasmic tail as bait.…”

Section: Discussionmentioning

confidence: 99%

“…To elucidate the signal transduction pathway of Fas-mediated apoptosis, several proteins have been isolated that associate with the cytoplasmic tail of Fas. These include the death domain-associated proteins, Fas-associated death domain (FADD) 3 (7)(8)(9), RIP (10), Fas-associated protein factor (FAF)-1 (11), ubiquitin conjugating enzyme (12,13), and Daxx (14). Both FADD and RIP also contain a death domain, and over-expression of either of them in cell lines results in apoptosis.…”

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confidence: 99%

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A Tailless Fas-FADD Death-Effector Domain Chimera Is Sufficient to Execute Fas Function in T Cells But Not B Cells of MRL-lpr/lprMice

Kabra

Cado

Winoto

1999

The Journal of Immunology

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The Fas receptor delivers signals crucial for lymphocyte apoptosis through its cytoplasmic death domain. Several Fas cytoplasmic-associated proteins have been reported and studied in cell lines. So far, only Fas-associated death domain protein (FADD), another death domain-containing molecule has been shown to be essential for Fas signals in vivo. FADD is thought to function by recruiting caspase-8 through its death-effector domain. To test whether FADD is sufficient to deliver Fas signals, we generated transgenic mice expressing a chimera comprised of the Fas extracellular domain and FADD death-effector domain. Expression of this protein in lymphocytes of Fas-deficient MRL-lpr/lpr mice completely diminishes their T cell but not their B cell abnormalities. These results suggest that FADD alone is sufficient for initiation of Fas signaling in primary T cells, but other pathways may operate in B cells.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

A Tailless Fas-FADD Death-Effector Domain Chimera Is Sufficient to Execute Fas Function in T Cells But Not B Cells of MRL-lpr/lprMice

Kabra

Cado

Winoto

1999

The Journal of Immunology

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“…Pharmrev Fast Forward. Published on 3 May 2023 as DOI 10.1124/pharmrev.122.000784 This article has at ASPET Journals on May 7, 2023 pharmrev.aspetjournals.org Downloaded from (Boddy et al, 1996;Matunis et al, 1996;Okura et al, 1996;Shen et al, 1996), SUMO2 (Mannen et al, 1996), SUMO3 (Lapenta et al, 1997), SUMO4 (Bohren et al, 2004;Guo et al, 2004), and SUMO5 (Liang et al, 2016), have been reported in the literature. An additional human SUMO6 can also be found in the NCBI Protein Database (Accession: QFR53058).…”

Section: A Sumo Isoformsmentioning

confidence: 99%

“…Small ubiquitin-like modifier (SUMO) was initially discovered around 1996 (Boddy et al, 1996;Matunis et al, 1996;Okura et al, 1996;Shen et al, 1996) and found as a covalent protein post-translational modification (PTM) attached to the Ran GTPase-activating protein (RanGAP1), in a manner similar to that of ubiquitination (Mahajan et al, 1997;Matunis et al, 1996). Protein SUMOylation is a conserved biological process essential for all eukaryotic organisms (Flotho and Melchior, 2013).…”

Section: Introductionmentioning

confidence: 99%

Paradoxes of Cellular SUMOylation Regulation: A Role of Biomolecular Condensates?

2023

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Protein SUMOylation is a major post-translational modification important for maintaining cellular homeostasis. SUMOylation has long been associated with stress responses as a diverse array of cellular stress signals are known to trigger rapid alternations in global protein SUMOylation. In addition, while there are large families of ubiquitination enzymes, all SUMOs are conjugated by a set of enzymatic machinery comprising one heterodimeric SUMO-activating enzyme, a single SUMO-conjugating enzyme, and a small number of SUMO protein ligases and SUMO-specific proteases. How a few SUMOylation enzymes specifically modify thousands of functional targets in response to diverse cellular stresses remains an enigma. Here, we review recent progress toward understanding the mechanisms of SUMO regulation, particularly, the potential roles of liquid-liquid phase separation/biomolecular condensates in the regulation of cellular SUMOylation during cellular stresses. In addition, we discuss the role of protein SUMOylation in pathogenesis and the development of novel therapeutics targeting SUMOylation. Significance Statement.Protein SUMOylation is one of the most prevalent post-translational modifications and plays an important role in maintaining cellular homeostasis in response to stresses. Protein SUMOylation has been implicated in human pathogenesis such as cancer, cardiovascular diseases, neurodegeneration, and infection. After more than a quarter century of extensive research, intriguing enigmas remain regarding the mechanism of cellular SUMOylation regulation and the therapeutic potential of targeting SUMOylation.

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“…The Small Ubiquitin like Modifier (SUMO) was discovered as a ubiquitin-like protein ( Boddy et al, 1996 ; Matunis et al, 1996 ; Okura et al, 1996 ; Mahajan et al, 1997 ), that is attached to a substrate by E1, E2 and E3 enzymes in a similar fashion as ubiquitin ( Gong et al, 1997 ; Johnson and Gupta, 2001 ; Kahyo et al, 2001 ; Pichler et al, 2002 ). In humans, three different functional SUMO isoforms (SUMO1-3) exist ( Gareau and Lima, 2010 ; Flotho and Melchior, 2013 ).…”

Section: The Sumo Pathwaymentioning

confidence: 99%

SUMO control of centromere homeostasis

Berg

Jansen

2023

Front. Cell Dev. Biol.

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Centromeres are unique chromosomal loci that form the anchorage point for the mitotic spindle during mitosis and meiosis. Their position and function are specified by a unique chromatin domain featuring the histone H3 variant CENP-A. While typically formed on centromeric satellite arrays, CENP-A nucleosomes are maintained and assembled by a strong self-templated feedback mechanism that can propagate centromeres even at non-canonical sites. Central to the epigenetic chromatin-based transmission of centromeres is the stable inheritance of CENP-A nucleosomes. While long-lived at centromeres, CENP-A can turn over rapidly at non-centromeric sites and even erode from centromeres in non-dividing cells. Recently, SUMO modification of the centromere complex has come to the forefront as a mediator of centromere complex stability, including CENP-A chromatin. We review evidence from different models and discuss the emerging view that limited SUMOylation appears to play a constructive role in centromere complex formation, while polySUMOylation drives complex turnover. The deSUMOylase SENP6/Ulp2 and the proteins segregase p97/Cdc48 constitute the dominant opposing forces that balance CENP-A chromatin stability. This balance may be key to ensuring proper kinetochore strength at the centromere while preventing ectopic centromere formation.

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Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin.

Cited by 287 publications

References 0 publications

A Tailless Fas-FADD Death-Effector Domain Chimera Is Sufficient to Execute Fas Function in T Cells But Not B Cells of MRL-lpr/lprMice

A Tailless Fas-FADD Death-Effector Domain Chimera Is Sufficient to Execute Fas Function in T Cells But Not B Cells of MRL-lpr/lprMice

Paradoxes of Cellular SUMOylation Regulation: A Role of Biomolecular Condensates?

SUMO control of centromere homeostasis

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