Regulatory subunit interactions of the 26S proteasome, a complex problem

Ferrell, Katherine; Wilkinson, Caroline R.M.; Dubiel, Wolfgang; Gordon, Colin

doi:10.1016/s0968-0004(99)01529-7

Cited by 215 publications

(152 citation statements)

References 49 publications

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“…Generally, the lid subcomplex encompasses eight stoichiometric subunits (RPN3, RPN5, RPN6, RPN7, RPN8, RPN9, RPN11, and RPN12) [17]. However, some non-essential subunits may transiently bind to the lid subcomplex in regulating 26S proteasome activity and localization [18,19]. In addition, the deubiquitinating enzymes (DUBs) that cleave the e-amide bond between ubiquitin and a lysine side chain to recycle the ubiquitin molecules from the substrate proteins are also found in the 19S subcomplex [16].…”

Section: The Ubiquitin/26s Proteasome Systemmentioning

confidence: 99%

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

et al. 2006

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Post-translational modification is central to protein stability and to the modulation of protein activity. Various types of protein modification, such as phosphorylation, methylation, acetylation, myristoylation, glycosylation, and ubiquitination, have been reported. Among them, ubiquitination distinguishes itself from others in that most of the ubiquitinated proteins are targeted to the 26S proteasome for degradation. The ubiquitin/26S proteasome system constitutes the major protein degradation pathway in the cell. In recent years, the importance of the ubiquitination machinery in the control of numerous eukaryotic cellular functions has been increasingly appreciated. Increasing number of E3 ubiquitin ligases and their substrates, including a variety of essential cellular regulators have been identified. Studies in the past several years have revealed that the ubiquitination system is important for a broad range of plant developmental processes and responses to abiotic and biotic stresses. This review discusses recent advances in the functional analysis of ubiquitination-associated proteins from plants and pathogens that play important roles in plant-microbe interactions.

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Section: The Ubiquitin/26s Proteasome Systemmentioning

confidence: 99%

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

et al. 2006

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“…Following binding, the 19S base unit performs the critical step of ATP-dependent unfolding of the substrate and 'feeding' it into the degradation chamber (Ferrell et al, 2000). The role of chaperonins, such as heat-shock proteins, in the recognition and unfolding process has yet to be fully evaluated, but the relation is close and has probably coevolved.…”

Section: Ubiquitinmentioning

confidence: 99%

“…What is clear is that many proteins have developed an affinity for the proteasome and bind to various subunits, most often within the 19S regulatory structure, to interfere with the degradative process. Since yeast two-hybrid screening is often used to detect such potential interactions, some may be artefactual, but many are real and have considerable potential for modulating proteasome function (Ferrell et al, 2000).…”

Section: Ubiquitinmentioning

confidence: 99%

“…Unlike the endosomal-lysosomal pathway, which operates in an acidic membrane-bound compartment, the proteasome is found in the cytosol, endoplasmic reticulum, and nucleus and is responsible for degrading the majority of endogenous cellular proteins (Ferrell et al, 2000;Pajonk and McBride, 2001c). It integrates its functions with other cellular processes, including the action of other proteases.…”

Section: Introductionmentioning

confidence: 99%

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The role of the ubiquitin/proteasome system in cellular responses to radiation

et al. 2003

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“…To narrow the TRC8 interaction domain in JAB1, we generated labeled proteins for amino acids 1 ± 187 containing the Nterminus and MPN protein interaction domain, the MPN domain alone (aa 55 ± 187), and the C-ter (aa 191 ± 327). Both proteins containing the MPN domain (Asano et al, 1997;Hofmann and Bucher, 1998;Ferrell et al, 2000) bound DTrc8 while the C-ter did not (Figure 4d, lower panels).…”

Section: Introductionmentioning

confidence: 99%

The TRC8 hereditary kidney cancer gene suppresses growth and functions with VHL in a common pathway

et al. 2002

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VHL is part of an SCF related E3-ubiquitin ligase complex with`gatekeeper' function in renal carcinoma. However, no mutations have been identi®ed in VHL interacting proteins in wild type VHL tumors. We previously reported that the TRC8 gene was interrupted by a t(3;8) translocation in a family with hereditary renal and non-medullary thyroid cancer. TRC8 encodes a multi-membrane spanning protein containing a RING-H2 ®nger with in vitro ubiquitin ligase activity. We isolated the Drosophila homologue, DTrc8, and studied its function by genetic manipulations and a yeast 2-hybrid screen. Human and Drosophila TRC8 proteins localize to the endoplasmic reticulum. Loss of either DTrc8 or DVhl resulted in an identical ventral midline defect. Direct interaction between DTrc8 and DVhl was con®rmed by GST-pulldown and co-immunoprecipitation experiments. CSN-5/JAB1 is a component of the COP9 signalosome, recently shown to regulate SCF function. We found that DTrc8 physically interacts with CSN-5 and that human JAB1 localization is dependent on VHL mutant status. Lastly, overexpression of DTrc8 inhibited growth consistent with its presumed role as a tumor suppressor gene. Thus, VHL, TRC8, and JAB1 appear to be linked both physically and functionally and all three may participate in the development of kidney cancer.

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Regulatory subunit interactions of the 26S proteasome, a complex problem

Cited by 215 publications

References 49 publications

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

The role of the ubiquitin/proteasome system in cellular responses to radiation

The TRC8 hereditary kidney cancer gene suppresses growth and functions with VHL in a common pathway

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