Induction of ubiquitin-conjugating enzymes during terminal erythroid differentiation.

Wefes, Inge; Mastrandrea, Lucy D.; Haldeman, Margaret T.; Koury, Stephen T.; Tamburlin, Judith; Pickart, Cecile M.; Finley, Daniel

doi:10.1073/pnas.92.11.4982

Cited by 72 publications

(61 citation statements)

References 56 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our observation that UBE2H is strongly induced during erythrocyte differentiation of human CD34 ϩ primary cells is also in line with previous results (52). It was also demonstrated that UBE2H expression is up-regulated during differentiation of erythroblasts to reticulocytes and reduced during terminal differentiation stages (53,54). A similar expression pattern was described for Tal1, which is highly expressed in early erythrocyte stages and down-regulated during later stages of maturation (55,56).…”

Section: Discussionsupporting

confidence: 79%

Targets of the Tal1 Transcription Factor in Erythrocytes

Lausen

Pleß

Leonard

et al. 2010

Journal of Biological Chemistry

View full text Add to dashboard Cite

The Tal1 transcription factor is essential for the development of the hematopoietic system and plays a role during definitive erythropoiesis in the adult. Despite the importance of Tal1 in erythropoiesis, only a small number of erythroid differentiation target genes are known. A chromatin precipitation and cloning approach was established to uncover novel Tal1 target genes in erythropoiesis. The BirA tag/BirA ligase biotinylation system in combination with streptavidin chromatin precipitation (Strep-CP) was used to co-precipitate genomic DNA bound to Tal1. Tal1 was found to bind in the vicinity of 31 genes including the E2-ubiquitin conjugase UBE2H gene. Binding of Tal1 to UBE2H was confirmed by chromatin immunoprecipitation. UBE2H expression is increased during erythroid differentiation of hCD34 ؉ cells. Tal1 expression activated UBE2H expression, whereas Tal1 knock-down reduced UBE2H expression and ubiquitin transfer activity. This study identifies parts of the ubiquitinylation machinery as a cellular target downstream of the transcription factor Tal1 and provides novel insights into Tal1-regulated erythropoiesis.

show abstract

Section: Discussionsupporting

confidence: 79%

Targets of the Tal1 Transcription Factor in Erythrocytes

Lausen

Pleß

Leonard

et al. 2010

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…It is ubiquitously expressed, but preferentially in brain, skeletal muscle and heart tissues [21]. In erythroid cells, UBE2O is upregulated during the reticulocyte stage of erythroid differentiation [22,23]. The function of UBE2O remains mostly unknown.…”

Section: Introductionmentioning

confidence: 99%

UBE2O negatively regulates TRAF6-mediated NF-κB activation by inhibiting TRAF6 polyubiquitination

Zhang

et al. 2013

Cell Res

View full text Add to dashboard Cite

Tumor necrosis factor (TNF) receptor-associated factor 6 (TRAF6) is a key regulator of the activation of transcription factor NF-κB by the interleukin-1 receptor (IL-1R)/Toll-like receptor (TLR) superfamily. Recruitment of TRAF6 to the receptor-associated IRAK1-IRAK4-MyD88 adaptor protein complex induces lysine 63 (K63) autopolyubiquitination of TRAF6, which leads to further recruitment of downstream regulators, such as TAB2/3 and TAK1, and subsequently triggers NF-κB activation. Here, we identified the putative E2 ubiquitin-conjugating (UBC) enzyme UBE2O as a novel negative regulator of TRAF6-dependent NF-κB signaling. We found that UBE2O binds to TRAF6 to inhibit its K63-polyubiquitination, and to prevent the activation of NF-κB by IL-1β and lipopolysaccharides (LPS). We further show that the inhibitory effect of UBE2O is independent of its carboxy-terminal UBC domain. In contrast, we found that UBE2O acts to disrupt the IL-1β-induced association of TRAF6 with MyD88. These results provide novel insight into the regulation of signaling by IL-1R/TLR and TRAF6.

show abstract

“…Ubiquitin, a small chaperone protein, is common to all eukaryotic cells and plays an important role in proteasomal and lysosomal protein degradation. Ubiquitin is thought to facilitate proteolysis and organelle degradation during reticulocyte differentiation (Rapoport & Schewe 1986, Wefes et al 1995. There is an indication that ubiquitin acts in synergy with the 15-LOX pathway during mitochondrial membrane degradation in the reticulocytes (Dubiel & Rapoport 1989, van Leyen et al 1998.…”

Section: Introductionmentioning

confidence: 99%

15-Lipoxygenase is a component of the mammalian sperm cytoplasmic droplet

Fischer¹,

Leyen²,

Lovercamp³

et al. 2005

Reproduction

View full text Add to dashboard Cite

Lipoxygenases (LOXs) are a family of enzymes capable of peroxidizing phospholipids. A member of the LOX family of enzymes, 15-LOX, participates in the degradation of mitochondria and other organelles within differentiating red blood cells, the reticulocytes. The present study provides biochemical and immunocytochemical evidence for the presence of 15-LOX in the sperm cytoplasmic droplet (CD). Testicular, epididymal and ejaculated spermatozoa were evaluated for the presence of 15-LOX using an affinity-purified immune serum raised against a synthetic peptide corresponding to the C-terminal sequence of rabbit reticulocyte 15-LOX. Western blotting revealed an appropriate single band of ,81 kDa in boar spermatozoa but not in boar seminal plasma. When ejaculated boar spermatozoa were subjected to separation on a 45/90% Percoll gradient, 15-LOX co-migrated with the immotile sperm and cellular debris/CD fractions, but not with the motile sperm fraction containing morphologically normal spermatozoa without CDs. Varied levels of 15-LOX were expressed in ejaculated sperm samples from boars with varied semen quality. By immunofluorescence, prominent 15-LOX immunoreactivity was found within the residual body in the testis and within the CDs from caput, corpus and cauda epididymal and ejaculated spermatozoa. Components of the ubiquitin-dependent proteolytic pathway, which is thought to facilitate both spermiogenesis and reticulocyte organelle degradation, were also detected in the sperm CD. These included ubiquitin, the ubiquitin-conjugating enzyme E2, the ubiquitin C-terminal hydrolase PGP 9.5, and various 20S proteasomal core subunits of the a-and b-type. The 15-LOX and various components of the ubiquitin-proteasome pathway were also detected in sperm CDs of other mammalian species, including the human, mouse, stallion and wild babirusa boar. We conclude that 15-LOX is prominently present in the mammalian sperm CD and thus may contribute to spermiogenesis, CD function or CD removal. Reproduction (2005) 130 213-222

show abstract

Induction of ubiquitin-conjugating enzymes during terminal erythroid differentiation.

Cited by 72 publications

References 56 publications

Targets of the Tal1 Transcription Factor in Erythrocytes

Targets of the Tal1 Transcription Factor in Erythrocytes

UBE2O negatively regulates TRAF6-mediated NF-κB activation by inhibiting TRAF6 polyubiquitination

15-Lipoxygenase is a component of the mammalian sperm cytoplasmic droplet

Contact Info

Product

Resources

About