Human ubiquitin‐protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin‐conjugating enzymes

Anan, Tadashi; Nagata, Yoichi; Koga, Hisashi; Honda, Yoshiomi; Yabuki, Nami; Miyamoto, Chikara; Kuwano, Atsutoshi; Matsuda, Ichiro; Endo, Fumio; Saya, Hideyuki; Nakao, Mitsuyoshi

doi:10.1046/j.1365-2443.1998.00227.x

Cited by 92 publications

(84 citation statements)

References 46 publications

(48 reference statements)

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“…Ubiquitylation is best known for its role in the selective degradation and/or processing of intracellular proteins in eukaryotic cells [143]. In conjunction with a series of enzymes namely, E1, E2 and E3 ligases, ubiquitin is prepared for conjugation to other proteins in an ATPdependent manner [135,144].…”

Section: The Redistribution Of Paxillin Between the Membrane Ruffle Amentioning

confidence: 99%

“…In conjunction with a series of enzymes namely, E1, E2 and E3 ligases, ubiquitin is prepared for conjugation to other proteins in an ATPdependent manner [135,144]. The conjugation of multiple ubiquitin molecules to a specific protein functions to target the protein for degradation by way of the 26S proteosomal pathway [143]. Consequently, like phosphorylation, ubiquitylation represents another post-translational modification that influences a wide variety of biological processes including, but not limited to gene expression, cellular stress response, antigen presentation, DNA repair, apoptosis, cell cycle and tumorigenesis [143,145].…”

Section: The Redistribution Of Paxillin Between the Membrane Ruffle Amentioning

confidence: 99%

“…The conjugation of multiple ubiquitin molecules to a specific protein functions to target the protein for degradation by way of the 26S proteosomal pathway [143]. Consequently, like phosphorylation, ubiquitylation represents another post-translational modification that influences a wide variety of biological processes including, but not limited to gene expression, cellular stress response, antigen presentation, DNA repair, apoptosis, cell cycle and tumorigenesis [143,145]. However, recent evidence suggests that the impact of ubiquitylation may be more far reaching than the proteasome: a comprehensive review of the subject by argues a non-proteolytic role for ubiquitin in the regulation of protein localization and activation [144,145].…”

Section: The Redistribution Of Paxillin Between the Membrane Ruffle Amentioning

confidence: 99%

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SLK-mediated phosphorylation of paxillin is required for focal adhesion turnover and cell migration

Baron

et al. 2012

Oncogene

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Section: The Redistribution Of Paxillin Between the Membrane Ruffle Amentioning

confidence: 99%

Section: The Redistribution Of Paxillin Between the Membrane Ruffle Amentioning

confidence: 99%

Section: The Redistribution Of Paxillin Between the Membrane Ruffle Amentioning

confidence: 99%

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SLK-mediated phosphorylation of paxillin is required for focal adhesion turnover and cell migration

Baron

et al. 2012

Oncogene

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“…This can occur as a consequence of direct mutation of PTEN gene itself and/or alteration of its degradation machinery, such as overexpression or superactivation of NEDD4-1. Indeed, it has been reported that NEDD4-1 expression level is very high in many human cancer cell lines (Anan et al, 1998), and it has also been documented to be highly overexpressed in a large cohort of human glioma samples (Oncomine database; Sun et al, 2006). Although the relationship of NEDD4-1 overexpression with PTEN in these gliomas is not clear, the important role of PTEN in gliomas warrants further investigation.…”

Section: Regulation Of Pten By Ubiquitinationmentioning

confidence: 99%

Post-translational regulation of PTEN

Wang

Jiang

2008

Oncogene

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PTEN (phosphatase and tensin homolog deleted on chromosome 10) tumor suppressor regulates a variety of cellular processes including cell proliferation, growth, migration and death. This master regulator itself is also under deliberative regulation. Although the evidence for PTEN regulation and its significance in normal biology and disease is overwhelming, the mechanisms and exact functional consequences of PTEN regulation are far from clear. In this review, we discuss recent advances concerning post-translational regulation of PTEN in general, and in more detail about its regulation by ubiquitination. We also discuss some unsolved questions in the field and how they might be addressed in the future. We propose that the complex regulatory mechanisms of PTEN dictate how this tumor suppressor executes its distinct biological functions.

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“…Permeases Gap1p and Fur4p are ubiquitylated at the cell membrane before being internalized by endocytosis (23)(24)(25). In addition, the human and mouse homologs of Rsp5, Nedd4, have been shown to be exclusively cytoplasmic (26,27). It will be interesting to determine the subcellular distribution of Rsp5.…”

Section: Fig 2 (A)mentioning

confidence: 99%

Transcription-coupled repair in yeast is independent from ubiquitylation of RNA pol II: Implications for Cockayne's syndrome

Lommel

Bucheli

Sweder

2000

Proc. Natl. Acad. Sci. U.S.A.

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Cockayne's syndrome cells lack transcription-coupled nucleotide excision repair (TCR) and ubiquitylation of RNA polymerase II large subunit (RNA pol II LS), suggesting that ubiquitylation of RNA pol II LS may be necessary for TCR in eukaryotes. Rsp5 is the sole yeast ubiquitin-protein ligase that ubiquitylates RNA pol II LS in cells exposed to DNA-damaging agents. In yeast lacking functional Rsp5, there is no ubiquitylation of RNA pol II LS. We show here that removal, repression, or over-expression of Rsp5 has no effect on TCR, demonstrating that ubiquitylation of the RNA pol II LS is not required for TCR. We infer that the lack of ubiquitylation of RNA pol II LS in Cockayne's syndrome cells does not cause their defect in TCR. C ockayne's syndrome (CS) is a rare autosomal recessive disorder displaying a variety of symptoms, including severe neurological abnormalities, dwarfism, deficiency of subcutaneous fat, and sun sensitivity (1). The UV sensitivity of CS patients and their cells in culture is thought to result from a deficiency in RNA synthesis (2), likely because of an inability to preferentially remove transcription-blocking DNA damage from the transcribed strands of expressed genes: i.e., impaired transcriptioncoupled repair (TCR) (3, 4).It has been shown that HeLa cells and normal human fibroblasts in culture ubiquitylate the large subunit of RNA polymerase II (RNA pol II LS) after exposure to UV radiation, cisplatin, mitomycin C, and methyl methanesulfonate (5). The ubiquitylation of RNA pol II LS was absent in UV-irradiated fibroblasts from CS patients. Interestingly, fibroblasts from patients displaying another autosomal recessive disorder associated with a DNA repair deficiency, xeroderma pigmentosum, were capable of ubiquitylating RNA pol II LS after UV irradiation (6). In both normal and xeroderma pigmentosum fibroblasts, the ubiquitylated form of RNA pol II LS was hyperphosphorylated, a form that is associated with the elongating transcription complex.Ubiquitin is a 76-amino acid peptide that gets linked via its terminal glycine (residue 76) to a cysteine residue of the ubiquitin-activating protein (E1) via a thioester bond. The ubiquityl moiety is then moved via transesterification from the E1 enzyme to a cysteine residue of one of the ubiquitin-conjugating enzymes (E2). Ubiquitin is then transferred via further transesterification to one or more -lysine residues in the acceptor or target protein. This step may require a ubiquitin-protein ligase, or E3. Finally, the recently identified E4 proteins bind ubiquitylated proteins and, together with E1, E2, and E3, facilitate formation of multiubiquitin chains on substrate proteins (7,8). Substrates of the ubiquitin system are degraded by the large 26S proteasome in an ATP-dependent fashion. Ubiquitylation may also serve a regulatory function independent of proteolysis. Ubiquitylation, through proteolysis and other mechanisms, plays a regulatory role in the cell cycle, cellular differentiation, stress responses, and many other cellular processes.In the...

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Human ubiquitin‐protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin‐conjugating enzymes

Cited by 92 publications

References 46 publications

SLK-mediated phosphorylation of paxillin is required for focal adhesion turnover and cell migration

SLK-mediated phosphorylation of paxillin is required for focal adhesion turnover and cell migration

Post-translational regulation of PTEN

Transcription-coupled repair in yeast is independent from ubiquitylation of RNA pol II: Implications for Cockayne's syndrome

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