Protein tyrosine nitration in the cell cycle

Jia, Min; Mateoiu, Claudia; Souchelnytskyi, Serhiy

doi:10.1016/j.bbrc.2011.08.084

Cited by 9 publications

(4 citation statements)

References 80 publications

(79 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is noted that palmitoylation of cyteines in proteins often occurs in multiple, closely associated cysteine residues. In addition to palmitoylation, there are other possible post translational modifications, such as tyrosine nitration [26], reported for TBC1D3, that could promote plasma membrane and lipid raft association.…”

Section: Discussionmentioning

confidence: 99%

Ubiquitination and degradation of the hominoid-specific oncoprotein TBC1D3 is regulated by protein palmitoylation

Chen

Lange

Samovski

et al. 2013

Biochemical and Biophysical Research Communications

View full text Add to dashboard Cite

Expression of the hominoid-specific oncoprotein TBC1D3 promotes enhanced cell growth and proliferation by increased activation of signal transduction through several growth factors. Recently we documented the role of CUL7 E3 ligase in growth factors-induced ubiquitination and degradation of TBC1D3. Here we expanded our study to discover additional molecular mechanisms that control TBC1D3 protein turnover. We report that TBC1D3 is palmitoylated on two cysteine residues: 318 and 325. The expression of double palmitoylation mutant TBC1D3:C318/325S resulted in protein mislocalization and enhanced growth factors-induced TBC1D3 degradation. Moreover, ubiquitination of TBC1D3 via CUL7 E3 ligase complex was increased by mutating the palmitoylation sites, suggesting that depalmitoylation of TBC1D3 makes the protein more available for ubiquitination and degradation. The results reported here provide novel insights into the molecular mechanisms that govern TBC1D3 protein degradation. Dysregulation of these mechanisms in-vivo could potentially result in aberrant TBC1D3 expression and promote oncogenesis.

show abstract

Section: Discussionmentioning

confidence: 99%

Ubiquitination and degradation of the hominoid-specific oncoprotein TBC1D3 is regulated by protein palmitoylation

Chen

Lange

Samovski

et al. 2013

Biochemical and Biophysical Research Communications

View full text Add to dashboard Cite

show abstract

“…com system by increasing blood flow and regulating intestinal flora (Hu et al 2020a;Wang et al 2020a), alleviating obesity by adjusting fat metabolism (Ma et al 2020a) and assisting tumor therapy by increasing sensitivity to cisplatin chemotherapy (Feng et al 2021a). Moreover, nitrate can significantly upregulate the expression of a variety of cellular signaling pathways, including the MAPK signaling pathway (Feng et al 2021b), the PI3K-Akt signaling pathway, the mTOR and WNT signaling pathway (Jiang et al 2014), glutathione metabolism, and the cell cycle (Jia et al 2011), which play important roles in cell regeneration, cell metabolism, and disease progression 3).…”

Section: Nitrogen Oxygen and Sialin-two Important Regulators In Homeo...mentioning

confidence: 99%

Homeostatic medicine: a strategy for exploring health and disease

Wang

Qin

2022

Curr Med

View full text Add to dashboard Cite

Homeostasis is a process of dynamic balance regulated by organisms, through which they maintain an internal stability and adapt to the external environment for survival. In this paper, we propose the concept of utilizing homeostatic medicine (HM) as a strategy to explore health and disease. HM is a science that studies the maintenance of the body’s homeostasis. It is also a discipline that investigates the role of homeostasis in building health, studies the change of homeostasis in disease progression, and explores ways to restore homeostasis for the prevention, diagnosis and treatment of disease at all levels of biological organization. A new dimension in the medical system with a promising future HM focuses on how homeostasis functions in the regulation of health and disease and provides strategic directions in disease prevention and control. Nitric oxide (NO) plays an important role in the control of homeostasis in multiple systems. Nitrate is an important substance that regulates NO homeostasis through the nitrate-nitrite-NO pathway. Sialin interacts with nitrate and participates in the regulation of NO production and cell biological functions for body homeostasis. The interactions between nitrate and NO or sialin is an important mechanism by which homeostasis is regulated.

show abstract

“…Moreover, ONOO − has been shown to positively activate pro-apoptotic proteins, such as poly (ADP-ribose) polymerase (PARP) [45, 46]. And though it is primarily implicated in pathologic and cell death-associated processes, there is growing evidence indicating that it also contributes during normal cellular physiology and may even serve as a positive regulator in cell signaling, and function in normal cell processes such as the cell cycle [47]. For example, low levels of ONOO − have been shown to enhance tyrosine phosphorylation signaling through inhibition of tyrosine phosphatases in vitro and in neurons [48, 49], and the Src tyrosine kinase and its associated signaling pathway undergo peroxynitrite-induced activation in neurons as well as erythrocytes [50, 51].…”

Section: Part 1 the Molecules Involved And Their Potential For Meanmentioning

confidence: 99%

The Good and Bad Effects of Cysteine S-nitrosylation and Tyrosine Nitration upon Insulin Exocytosis: A Balancing Act

Wiseman

Thurmond²

2012

CDR

View full text Add to dashboard Cite

As understanding of the mechanisms driving and regulating insulin secretion from pancreatic beta cells grows, there is increasing and compelling evidence that nitric oxide (•NO) and other closely-related reactive nitrogen species (RNS) play important roles in this exocytic process. •NO and associated RNS, in particular peroxynitrite, possess the capability to effect signals across both intracellular and extracellular compartments in rapid fashion, affording extraordinary signaling potential. It is well established that nitric oxide signals through activation of guanylate cyclase-mediated production of cyclic GMP. The intricate intracellular redox environment, however, lends credence to the possibility that •NO and peroxynitrite could interact with a wider variety of biological targets, with two leading mechanisms involving 1) S-nitrosylation of cysteine, and 2) nitration of tyrosine residues comprised within a variety of proteins. Efforts aimed at delineating the specific roles of •NO and peroxynitrite in regulated insulin secretion indicate that a highly-complex and nuanced system exists, with evidence that •NO and peroxynitrite can contribute in both positive and negative regulatory ways in beta cells. Furthermore, the ultimate biochemical outcome within beta cells, whether to compensate and recover from a given stress, or not, is likely a summation of contributory signals and redox status. Such seeming regulatory dichotomy provides ample opportunity for these mechanisms to serve both physiological and pathophysiologic roles in onset and progression of diabetes. This review focuses attention upon recent accumulating evidence pointing to roles for nitric oxide induced post-translational modifications in the normal regulation as well as the dysfunction of beta cell insulin exocytosis.

show abstract

Protein tyrosine nitration in the cell cycle

Cited by 9 publications

References 80 publications

Ubiquitination and degradation of the hominoid-specific oncoprotein TBC1D3 is regulated by protein palmitoylation

Ubiquitination and degradation of the hominoid-specific oncoprotein TBC1D3 is regulated by protein palmitoylation

Homeostatic medicine: a strategy for exploring health and disease

The Good and Bad Effects of Cysteine S-nitrosylation and Tyrosine Nitration upon Insulin Exocytosis: A Balancing Act

Contact Info

Product

Resources

About