Changes in Three Types of Ubiquitin mRNA and Ubiquitin-protein Conjugate Levels During Lens Development

Yang, Sen; Wang-Su, Shuh-Tuan; Cai, Huicong; Wagner, B.J.

doi:10.1006/exer.2001.1149

Cited by 10 publications

(5 citation statements)

References 47 publications

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“…Previous studies support a developmental regulation of ubiquitin conjugation in the nervous system and indicate that protein degradation by the proteasome is required for normal neuronal development (Yang et al, 2002; Flann et al, 1997). The NMJ undergoes a massive rearrangement in size and structure during postnatal development and transforms from a small “plaque-like” structure to a large “pretzel-like” structure (Sanes and Lichtman 1999).…”

Section: Discussionmentioning

confidence: 68%

Ubiquitin Homeostasis Is Critical for Synaptic Development and Function

Bhattacharyya²,

et al. 2011

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The ubiquitin-proteasome system (UPS) controls protein abundance and is essential for many aspects of neuronal function. In ataxia (ax J ) mice, profound neurological and synaptic defects result from a loss-of-function mutation in the proteasome-associated deubiquitinating enzyme Usp14, which is required for recycling ubiquitin from proteasomal substrates. Here, we show that transgenic complementation of ax J mice with neuronally expressed ubiquitin prevents early postnatal lethality, restores muscle mass, and corrects developmental and functional deficits resultingfromthelossofUsp14,demonstratingthatubiquitindeficiencyisamajorcauseoftheneurologicaldefectsobservedinthe ax J mice.We also show that proteasome components are normally induced during the first 2 weeks of postnatal development, which coincides with dramatic alterations in polyubiquitin chain formation. These data demonstrate a critical role for ubiquitin homeostasis in synaptic development and function, and show that ubiquitin deficiency may contribute to diseases characterized by synaptic dysfunction.

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Section: Discussionmentioning

confidence: 68%

Ubiquitin Homeostasis Is Critical for Synaptic Development and Function

Bhattacharyya²,

et al. 2011

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“…In lens homogenates, characterization of different proteolytic systems, especially the proteasome, has been the subject of many studies starting with reports from van Heyningens's group [9,12,[25][26][27][28][29]. Experimental results [5] have suggested that cataract formation may be linked to decreased activity of the proteasome leading to development of light-scattering aggregates, which thereby will destroy the transparency of the lens.…”

Section: Discussionmentioning

confidence: 99%

“…The involvement of these proteases in processes related to cataractogenesis has been shown for cultured cells [7], lens epithelial explants [8,9], cell lysates [6,10,11] and homogenized lenses [12]. An approach more similar to the in vivo situation is to monitor the protease systems in the intact lens with the proteases in their normal subcellular localization and the lens epithelium and lens fibers still intact.…”

Section: Introductionmentioning

confidence: 99%

A New Model for Assessing Proteolysis in the Intact Mouse Lens in Organ Culture

et al. 2004

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Purpose: To develop a new method to investigate proteolysis in the intact lens in organ culture. Methods: Intact mouse lenses were assayed at regular intervals for proteolytic activity using fluorogenic peptide substrates ± addition of ionomycin. Specific inhibitors were used to determine the activity of calpains, the proteasome and acid lysosomal enzymes. Results: Significant levels of proteolytic activity were present in the intact lens. Proteolysis was stimulated by ionomycin. Preincubation with an inhibitor to the proteasome significantly decreased proteolysis whereas inhibitors of calpain and acid lysosomal enzymes did not. Conclusion: This study indicates that in the intact mouse lens in culture, the proteasome is an important protease. Its activity is at least partially regulated by calcium.

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“…The ubiquitin pathway has been most thoroughly characterized in the yeast Saccharomyces cerevisiae, where it is important both in mediating cell differentiation and in responses to stress (Hilt and Wolf 1995). In plants and animals, there is increasing biochemical and molecular evidence for involvement of the ubiquitin pathway in development and responses to stress (Yang et al 2002;Laney and Hochstrasser 2004;Maeda et al 2004).…”

Section: Introductionmentioning

confidence: 99%

Cloning and characterization of two types of ubiquitin genes from Gracilariopsis lemaneiformis (Gracilariales, Rhodophyta)

et al. 2008

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Two types of ubiquitin genes were isolated from the marine red alga Gracilaria lemaneiformis: a ubiquitin-52 amino acid fusion protein gene, and a 6-unit polyubiquitin gene. Alignment of polyubiquitins among three red algae (Gracilaria lemaneiformis, Gracilaria verrucosa, Aglaothamnion neglectum) and other species revealed that there were six ubiquitin repeats in all three red algae polyubiquitins, and that glutamine was the final amino acid residue in the terminal repeat of the polyprotein in the two Gracilaria sequences. Southern blot analysis revealed that both genes were encoded by low-copy number genes. Semi-quantitative RT-PCR was performed to investigate the expression of these two genes in two phases of G. lemaneiformis. The result revealed that the monoubiquitin was phase-relative, and upregulated in tetrasporophytes compared with female gametophytes. The polyubiquitin gene was expressed at similar levels in both phases.

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Changes in Three Types of Ubiquitin mRNA and Ubiquitin-protein Conjugate Levels During Lens Development

Cited by 10 publications

References 47 publications

Ubiquitin Homeostasis Is Critical for Synaptic Development and Function

Ubiquitin Homeostasis Is Critical for Synaptic Development and Function

A New Model for Assessing Proteolysis in the Intact Mouse Lens in Organ Culture

Cloning and characterization of two types of ubiquitin genes from Gracilariopsis lemaneiformis (Gracilariales, Rhodophyta)

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