Differential directing of c-Fos and c-Jun proteins to the proteasome in serum-stimulated mouse embryo fibroblasts

Salvat, Catherine; Jariel-Encontre, Isabelle; Acquaviva, Claire; Ōmura, Satoshi; Piechaczyk, Marc

doi:10.1038/sj.onc.1201922

Cited by 37 publications

(45 citation statements)

References 37 publications

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“…Under conditions of constitutive expression, which are those of FBJ-MSV and FBR-MSV-transduced fos genes, c-Fos degradation is fully inhibited in the presence of MG132, indicating that proteasomal degradation of c-Fos is not restricted to the G 0 -to-S phase transition (Salvat et al, 1998) but can occur during other phases of the cell cycle. In contrast, vFos FBJ and v-Fos FBR are longer-lived and have acquired resistance to the proteasome.…”

Section: Distinct Sequence Determinants Are Responsible For the Resismentioning

confidence: 98%

“…Thus, c-Fos can be ubiquitinylated by puri®ed or semi-puri®ed ubiquitinylation enzymes in vitro (Hermida-Matsumoto et al, 1996;Stancovski et al, 1995) and is slightly stabilized in one mutant cell line (hamster E36-ts20 cell line) thermosensitive for the ubiquitin pathway when cultured at the restrictive temperature (Stancovski et al, 1995). However, it is not stabilized (Salvat et al, 1998) in another thermosensitive cell mutant (mouse A31N-ts20 cells) (Salvat et al, 2000) and c-Fos-ubiquitin conjugates have, thus far, not been described in vivo.…”

Section: Introductionmentioning

confidence: 99%

“…Z-VAD-FMK (100 mM, Sigma RBI) was added to the culture medium 1 h before the pulse. Conditions for the use of MG132, calpain inhibitor II, E64D and chloroquine were described elsewhere (Palombella et al, 1994;Salvat et al, 1998). Z-VAD-FMK and AAF-CMK were shown to inhibit the activity of caspases and serine proteases, respectively, by 490 ± 95% under the experimental conditions used.…”

Section: Cell Transfection Pulse-chase Experiments and Protease Inhimentioning

confidence: 99%

“…Cos-7 cells were obtained from the American Type Culture Collection (Bethesda, MD, USA) and were grown in highglucose Dulbecco's modi®ed Eagle medium (Gibco/BRL) under standard conditions (Salvat et al, 1998). Transient transfections were performed using the calcium phosphate coprecipitation procedure (Sambrook et al, 1989) using 5 ± 20 mg of expression vector per 2610 6 cells.…”

Section: Cell Transfection Pulse-chase Experiments and Protease Inhimentioning

confidence: 99%

“…Most often, but not always (Verma and Deshaies, 2000), the addressing to the proteasome requires conjugation of multiubiquitin chains to protein substrates . The proteasome has been shown to play a crucial role in c-Fos destruction in mouse and human ®broblasts during the G 0 -to-S phase transition (Salvat et al, 1998) and in a lymphoma cell line undergoing apoptosis (He et al, 1998). Lysosomes and calpains have also been suggested to contribute to cFos breakdown (Aniento et al, 1996;Carillo et al, 1994;Hirai et al, 1991;Salvat et al, 1999;Watt and Molloy, 1993).…”

Section: Introductionmentioning

confidence: 99%

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Cellular and viral Fos proteins are degraded by different proteolytic systems

et al. 2001

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c-Fos proto-oncoprotein is a short-lived transcription factor degraded by the proteasome in vivo. Its mutated forms expressed by the mouse osteosarcomatogenic retroviruses, FBJ-MSV and FBR-MSV, are stabilized two-and threefold, respectively. To elucidate the mechanisms underlying v-Fos FBJ and v-Fos FBR protein stabilization, we conducted a genetic analysis in which the half-lives and the sensitivities to various cell-permeable protease inhibitors of a variety of cellular and viral protein mutants were measured. Our data showed that the decreased degradation of v-Fos FBJ and v-Fos FBR is not simply explained by the deletion of a c-Fos destabilizing C-terminal domain. Rather, it involves a complex balance between opposing destabilizing and stabilizing mutations which are distinct and which include virallyintroduced peptide motifs in both cases. The mutations in viral Fos proteins conferred both total insensitivity to proteasomal degradation and sensitivity to another proteolytic system not naturally operating on c-Fos, explaining the limited stabilization of the two proteins. This observation is consistent with the idea that FBR-MSV and FBJ-MSV expression machineries have evolved to ensure controlled protein levels. Importantly, our data illustrate that the degradation of unstable proteins does not necessarily involve the proteasome and provide support to the notion that highly related proteins can be broken down by di erent proteolytic systems in living cells. Oncogene (2001) 20, 942 ± 950.

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Section: Distinct Sequence Determinants Are Responsible For the Resismentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Section: Cell Transfection Pulse-chase Experiments and Protease Inhimentioning

confidence: 99%

Section: Cell Transfection Pulse-chase Experiments and Protease Inhimentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Cellular and viral Fos proteins are degraded by different proteolytic systems

et al. 2001

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SUMO4 and its role in type 1 diabetes pathogenesis

Wang¹,

She²

2008

Diabetes Metabolism Res

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Susceptibility to type 1 diabetes (T1D) is determined by interactions of multiple genes with unknown environmental factors. Despite the characterization of over 20 susceptibility regions for T1D, identification of specific genes in these regions is still a formidable challenge. In 2004, we first reported the cloning of a novel, small ubiquitin-like modifier (SUMO) gene, SUMO4, in the IDDM5 interval on chromosome 6q25, and presented strong genetic and functional evidence suggesting that SUMO4 is a T1D susceptibility gene. Subsequent studies have consistently confirmed this association in multiple Asian populations despite controversial observations in Caucasians. In this review, we will update the genetic evidence supporting SUMO4 as a T1D susceptibility gene and discuss the possible explanations for the discrepant associations observed in Caucasians. We will then discuss the mechanisms through which SUMO4 contributes to the pathogenesis of T1D.

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