Non-traditional Functions of Ubiquitin and Ubiquitin-binding Proteins

Schnell, Joshua D.; Hicke, Linda A

doi:10.1074/jbc.r300018200

Cited by 386 publications

(310 citation statements)

References 67 publications

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“…Thus, understanding of when and where (i.e., at what level) ubiquitination operates in regulating plant defenses could be of equal importance to the determination of which substrates are targeted. It is noteworthy that ubiquitinated substrate proteins not necessarily are targeted for degradation [119]. Mono-ubiquitination or non-canonical ubiquitination might also be employed to fine tune the function of modified substrate proteins in plant-pathogen interactions.…”

Section: Discussionmentioning

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: Discussionmentioning

confidence: 99%

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

et al. 2006

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“…As a general rule any protein bearing a lysine-48 linked chain of at least 4 Ub moieties is degraded by the proteasome (32,33). In contrast, a common feature of many non-proteasomal functions of Ub is that the substrate protein is modified by only a single Ub i.e., monoubiquitinated (34,35). Recently bioinformatic approaches have shown that a number of downstream effectors are involved in the non-proteolyitc functions of Ub.…”

Section: Ubiquitin-proteasome Pathway (Upp)mentioning

confidence: 99%

“…Mono and di-ubiquitination has been implicated in endocytosis, histone regulation and budding of retroviruses. Ubiquitin is now known to participate in protein trafficking to endosomal compartments either from plasma membrane, or from the trans-Golgi network (34,35).…”

Section: Ubiquitin-proteasome Pathway (Upp)mentioning

confidence: 99%

Nuclear hormone receptor degradation and gene transcription: An update

Ismail

Nawaz

2005

IUBMB Life (International Union of Biochemistry and Molecular B

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SummaryThe ubiquitin-proteasome pathway (UPP) is known to degrade short-lived and misfolded proteins. Its role in cell cycle regulation and signal transduction is well established. However, the importance of the UPP in nuclear hormone receptor-regulated gene transcription is relatively new. Nuclear hormone receptors (NHRs) are degraded by the UPP both in the presence or absence of their cognate ligands. In recent years, it has become evident that NHR degradation and NHR-dependent transcription are interdependent processes. The link between these two processes has become stronger with the discovery of a number of ubiquitin-pathway enzymes and components of the proteasome acting as modulators of NHR function. Also, UPP enzymes and components of the proteasome are recruited to the promoters of NHR-responsive genes. Interestingly both coactivators and corepressors (coregulators) of NHRs are also targeted to the UPP for degradation. Furthermore, additional evidence also indicates that the UPP may be involved in the turnover of transcription complexes, thereby facilitating proper gene transcription. In this review we discuss and provide an update on the role of UPP in NHR-dependent gene regulation. IUBMB Life, 57: 483 -490, 2005

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“…Many post translation modifications like nitrosylation, nitration and even ubiquitination of signaling proteins seem to play important role in transducing the signal Lane et al 2001;Schnell and Hicke 2003;Ischiropoulos 2003). These modifications seem to act by altering the protein stability, localization or protein-protein association.…”

Section: Introductionmentioning

confidence: 99%

Effect of nitric oxide donor and gamma irradiation on modifications of ERK and JNK in murine peritoneal macrophages

Narang

Dhariwala

Krishna

2007

J. Cell Commun. Signal.

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Mitogen activated protein kinases (MAPKs) play an important role in activation, differentiation and proliferation of macrophages. Macrophages, upon activation, produce large amounts of nitric oxide that inhibit the growth of variety of microorganisms and tumor cells. This nitric oxide which is known to interfere with tyrosine phosphorylation may result in changes in the pattern of activation of MAPKs. In a previous study we have found that tyrosine phosphorylation of MAPKs was completely abolished in the presence of nitric oxide donor and radiation but this did not affect the function of macrophages. In this study the other post translational modifications namely nitration and ubiquitination of JNK and ERK have been looked at. Both ERK and JNK were found to be nitrated. However, there was no increase in ubiquitination of ERK and JNK, indicating that ubiquitination, in this case was not a natural consequence of nitration and may serve in signaling. Additionally, when the nitration was extensive, phosphorylation was also inhibited. The activation of substrates of ERK and JNK were looked at to determine the consequences of such modifications. Inhibition of phosphorylation and extensive nitration of JNK did not prevent activation of its substrate, c-jun. This study indicates that ERK and JNK may be under regulation by different type of modifications in macrophages.

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Non-traditional Functions of Ubiquitin and Ubiquitin-binding Proteins

Cited by 386 publications

References 67 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

Nuclear hormone receptor degradation and gene transcription: An update

Effect of nitric oxide donor and gamma irradiation on modifications of ERK and JNK in murine peritoneal macrophages

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