Wyniki wyszukiwania

1

On the spatial organization of ubiquitin-dependent proteolysis in HeLa cells

100%

Wojcik C.

Folia Histochemica et Cytobiologica

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1997

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tom 35

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nr 2

2

Occurrence of ubiquitin during spermiogenesis in Chara vulgaris

86%

Kwiatkowska M., Wojtczak A., Poplonska K., Gosek A.

Folia Histochemica et Cytobiologica

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2001

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tom 39

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nr 2

3

Erythrocyte spectrin is an E2 ubiquitin conjugating enzyme

86%

Goodman S. R., Kakhniashvili D. G., Sangerman J., Chaudhary T., Zimmer W. E., Bencsath F. A., Jardine I.

Cellular and Molecular Biology Letters

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2001

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tom 06

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nr 2

4

Developmental regulation of Ubc9 in the rat nervous system

72%

Watanabe M., Takahashi K., Tomizawa K., Mizusawa H., Takahashi H.

Acta Biochimica Polonica

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2008

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tom 55

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nr 4

681-686

The SUMO-conjugating enzyme Ubc9 is an essential enzyme in the SUMO (small ubiquitin-related modifier) protein modification system. Although sumoylation, covalent modification of cellular proteins by SUMO, is considered to regulate various cellular processes, and many substrates for sumoylation have been identified recently, the regulation of Ubc9 expression has not been examined in detail. We analyzed the expression of Ubc9 during rat brain development at the mRNA and protein levels. Northern and Western blot analyses revealed that expression of Ubc9 and SUMO-1 was developmentally regulated, while that of the ubiquitin-conjugating enzyme UbcH7 did not change so dramatically. In situ hybridization analysis revealed that the expression of Ubc9 was high in neuronal stem cells and moderate in differentiated neurons at embryonic stages. In the adult brain, moderate expression was observed in subsets of neurons, such as the dentate granular neurons and pyramidal neurons in the hippocampal formation and the large pyramidal neurons in the cerebral cortex. These results suggest that the Ubc9-SUMO system might participate in the proliferation and differentiation of neuronal cells in the developing brain and in neuronal plasticity in the adult brain.

5

The role of the ubiquitin/ 26S proteasome pathway in plant morphogenesis and embryogenesis

72%

Brukhin V., Thomann A., Dieterle M., Gheyselinck J., Genschik P., Grossniklaus U.

Acta Biologica Cracoviensia. Series Botanica. Supplement

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2005

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tom 47

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nr 1

6

Accumulation of aquaporin-1 during hemolysin-induced necrotic cell death

72%

Schweitzer K., Li E., Sidhaye V., Leitch V., Kuznetsov S., King L. S.

Cellular and Molecular Biology Letters

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2008

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tom 13

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nr 2

195-211

Altered tissue water homeostasis may contribute to edema formation during various stresses including bacterial infection. We observed induction of aquaporin-1 (AQP1) during Staphylococcus aureus infection of cultured cells indicating a potential mechanism underlying altered water homeostasis during infection. To investigate mechanisms of AQP1 induction, we examined the effects of the S. aureus alpha-hemolysin on AQP1 abundance in Balb/c fibroblasts. Fibroblasts incubated with 30 microg/ml hemolysin exhibited a 5-10 fold increase in AQP1 protein within 4-6 hours of exposure. The use of multiple signaling cascade inhibitors failed to affect hemolysin-mediated accumulation of AQP1. However, immunoprecipitation revealed an initial accumulation of ubiquitinated AQP1 followed by a decrease to baseline levels after 4 hours. Immunofluorescence indicated that following hemolysin exposure, AQP1 was no longer on the plasma membrane, but was found in a population of submembrane vacuoles. AQP1 redistribution was further indicated by surface biotinylation experiments suggesting diminished AQP1 abundance on the plasma membrane as well as redistribution out of lipid raft fractions. Live cell confocal microscopy revealed that the pattern of cell volume change observed following hemolysin exposure was altered in cells in which AQP1 was silenced. We conclude that alpha-toxin alters proteasomal processing and leads to intracellular accumulation of AQP1, which may likely contribute to disrupted cell volume homeostasis in infection.

7

Proteasomes, ubiquitin and the effects of epoxomicin, an inhibitor of proteasomal proteolytic activity, on the spermiogenesis of Chara vulgaris

72%

Kwiatkowska M., Poplonska K., Wojtczak A., Gosek A., Stepinski D.

Cellular and Molecular Biology Letters

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2002

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tom 07

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nr Suppl.

8

Degradation and beyond: control of androgen receptor activity by the proteasome system

72%

Jaworski T.

Cellular and Molecular Biology Letters

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2006

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tom 11

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nr 1

The androgen receptor (AR) is a transcription factor belonging to the family of nuclear receptors which mediates the action of androgens in the development of urogenital structures. AR expression is regulated post-translationally by the ubiquitin/proteasome system. This regulation involves more complex mechanisms than typical degradation. The ubiquitin/proteasome system may regulate AR via mechanisms that do not engage in receptor turnover. Given the critical role of AR in sexual development, this complex regulation is especially important. Deregulation of AR signalling may be a causal factor in prostate cancer development. AR is the main target in prostate cancer therapies. Due to the critical role of the ubiquitin/proteasome system in AR regulation, current research suggests that targeting AR degradation is a promising approach.

Ograniczanie wyników

On the spatial organization of ubiquitin-dependent proteolysis in HeLa cells

Occurrence of ubiquitin during spermiogenesis in Chara vulgaris

Erythrocyte spectrin is an E2 ubiquitin conjugating enzyme

Developmental regulation of Ubc9 in the rat nervous system

The role of the ubiquitin/ 26S proteasome pathway in plant morphogenesis and embryogenesis

Accumulation of aquaporin-1 during hemolysin-induced necrotic cell death

Proteasomes, ubiquitin and the effects of epoxomicin, an inhibitor of proteasomal proteolytic activity, on the spermiogenesis of Chara vulgaris

Degradation and beyond: control of androgen receptor activity by the proteasome system