Regulation of Egr-1 by association with the proteasome component C8

Bae, Myung-Ho; Jeong, Chul‐Ho; Kim, Sehee; Bae, Moon‐Kyoung; Jeong, Joo‐Won; Ahn, Mee‐Young; Bae, Soo-Kyung; Kim, Nam Deuk; Kim, Chul Woo; Kim, Kwang-Rok; Kim, Kyu‐Won

doi:10.1016/s0167-4889(02)00310-5

Cited by 37 publications

(26 citation statements)

References 24 publications

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“…EGR-1 and DUSP-1 can also be up-regulated by a variety of other stimuli representing both internal and external cell stress factors that may include pathogens/microorganisms, temperature, hypoxia, oxidative stress, or inflammatory mediators (Parra et al, 2011;Hammer et al, 2006). Deregulated expression of EGR-1 and DUSP-1 has also been linked to allergy-associated processes, such as cell adhesion (Liu et al, 1999), cell/tissue repair (Guerquin et al, 2013), wound healing (Braddock, 2001), control of protease inhibitors expression (Bae et al, 2002), immune modulation (Caceres et al, 2013), and cell recruitment (Rodriguez et al, 2010). Consequently, it does not come as a surprise that these transcription factors may also play a role in an allergic setting.…”

Section: Discussionmentioning

confidence: 99%

EGR-1 and DUSP-1 are important negative regulators of pro-allergic responses in airway epithelium

Golebski

Egmond

Groot

et al. 2015

Molecular Immunology

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Section: Discussionmentioning

confidence: 99%

EGR-1 and DUSP-1 are important negative regulators of pro-allergic responses in airway epithelium

Golebski

Egmond

Groot

et al. 2015

Molecular Immunology

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“…Similarly, EGR1 can be acetylated by the histone acetyltransferase complex p300/CBP, which reduces its transcriptional activity (Yu et al, 2004). Interestingly, EGR1 can undergo sumoylation and ubiquitination, and has been reported to interact directly with proteasome component C8, describing a likely mechanism controlling its targeting for proteolysis by the ubiquitin-dependent proteasome pathway (Bae et al, 2002; Li et al, 2015). Notably, such regulation has been observed following stimulation of ECV304 cells by epidermal growth factor, which increases sumoylation and ubiquitination levels of endogenous EGR1 proteins, ultimately leading to higher EGR1 turnover through proteasome-mediated degradation (Manente et al, 2011).…”

Section: Functions and Regulations Of Egr1mentioning

confidence: 99%

The Role of Early Growth Response 1 (EGR1) in Brain Plasticity and Neuropsychiatric Disorders

Duclot

Kabbaj

2017

Front. Behav. Neurosci.

282

240

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It is now clearly established that complex interactions between genes and environment are involved in multiple aspects of neuropsychiatric disorders, from determining an individual’s vulnerability to onset, to influencing its response to therapeutic intervention. In this perspective, it appears crucial to better understand how the organism reacts to environmental stimuli and provide a coordinated and adapted response. In the central nervous system, neuronal plasticity and neurotransmission are among the major processes integrating such complex interactions between genes and environmental stimuli. In particular, immediate early genes (IEGs) are critical components of these interactions as they provide the molecular framework for a rapid and dynamic response to neuronal activity while opening the possibility for a lasting and sustained adaptation through regulation of the expression of a wide range of genes. As a result, IEGs have been tightly associated with neuronal activity as well as a variety of higher order processes within the central nervous system such as learning, memory and sensitivity to reward. The immediate early gene and transcription factor early growth response 1 (EGR1) has thus been revealed as a major mediator and regulator of synaptic plasticity and neuronal activity in both physiological and pathological conditions. In this review article, we will focus on the role of EGR1 in the central nervous system. First, we will summarize the different factors influencing its activity. Then, we will analyze the amount of data, including genome-wide, that has emerged in the recent years describing the wide variety of genes, pathways and biological functions regulated directly or indirectly by EGR1. We will thus be able to gain better insights into the mechanisms underlying EGR1’s functions in physiological neuronal activity. Finally, we will discuss and illustrate the role of EGR1 in pathological states with a particular interest in cognitive functions and neuropsychiatric disorders.

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“…Several studies have reported that binding to Psma3 results in protein degradation by proteasome in a ubiquitin-independent pathway (73)(74)(75)(76). Moreover, investigators found that proteins binding to Psma3 can undergo proteasome cleavage to form truncated fragments that retain biological activity (60).…”

Section: Discussionmentioning

confidence: 99%

Protein Interaction between Ameloblastin and Proteasome Subunit α Type 3 Can Facilitate Redistribution of Ameloblastin Domains within Forming Enamel

Geng

White

Paine

et al. 2015

Journal of Biological Chemistry

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Background: Ameloblastin domain redistribution during development serves to pattern mineral microstructure. Results: Proteasome subunit ␣ type 3 (Psma3) interacts with the C terminus of ameloblastin, and the 20S proteasome can digest ameloblastin. Conclusion: Ameloblastin-Psma3 interaction facilitates ameloblastin domain separation and redistribution defining the enamel rod boundaries. Significance: This study investigates the mechanism of enamel microstructural formation at the level of protein-to-protein interaction.

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Regulation of Egr-1 by association with the proteasome component C8

Cited by 37 publications

References 24 publications

EGR-1 and DUSP-1 are important negative regulators of pro-allergic responses in airway epithelium

EGR-1 and DUSP-1 are important negative regulators of pro-allergic responses in airway epithelium

The Role of Early Growth Response 1 (EGR1) in Brain Plasticity and Neuropsychiatric Disorders

Protein Interaction between Ameloblastin and Proteasome Subunit α Type 3 Can Facilitate Redistribution of Ameloblastin Domains within Forming Enamel

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