Post-translational modifications on yeast carbon metabolism: Regulatory mechanisms beyond transcriptional control

2015 ◽  
Vol 1850 (4) ◽  
pp. 620-627 ◽  
Author(s):  
Farida Tripodi ◽  
Raffaele Nicastro ◽  
Veronica Reghellin ◽  
Paola Coccetti
Keyword(s):  
Carbon Metabolism ◽  
Transcriptional Control ◽  
Regulatory Mechanisms ◽  
Post Translational Modifications

scholarly journals Identification, Characterization, and Regulatory Mechanisms of a Novel EGR1 Splicing Isoform

2019 ◽  
Vol 20 (7) ◽  
pp. 1548 ◽  
Author(s):  
Vincenza Aliperti ◽  
Giulia Sgueglia ◽  
Francesco Aniello ◽  
Emilia Vitale ◽  
Laura Fucci ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Cell Types ◽  
Regulatory Mechanisms ◽  
Brain Diseases ◽  
Regulation Of Transcription ◽  
Biological Processes ◽  
Activation Domain ◽  
Post Translational Modifications ◽  
Pathological Conditions ◽  
Proliferation And Apoptosis

EGR1 is a transcription factor expressed in many cell types that regulates genes involved in different biological processes including growth, proliferation, and apoptosis. Dysregulation of EGR1 expression has been associated with many pathological conditions such as tumors and brain diseases. Known molecular mechanisms underlying the control of EGR1 function include regulation of transcription, mRNA and protein stability, and post-translational modifications. Here we describe the identification of a splicing isoform for the human EGR1 gene. The newly identified splicing transcript encodes a shorter protein compared to the canonical EGR1. This isoform lacks a region belonging to the N-terminal activation domain and although it is capable of entering the nucleus, it is unable to activate transcription fully relative to the canonical isoform.

scholarly journals Post-Translational Modification-Dependent Activity of Matrix Metalloproteinases

2019 ◽  
Vol 20 (12) ◽  
pp. 3077 ◽  
Author(s):  
Elizabeta Madzharova ◽  
Philipp Kastl ◽  
Fabio Sabino ◽  
Ulrich auf dem Keller
Keyword(s):  
Matrix Metalloproteinases ◽  
Transcriptional Control ◽  
Proteolytic Processing ◽  
Post Translational Modification ◽  
Proteolytic Activation ◽  
Control Of Gene Expression ◽  
Post Translational Modifications ◽  
Binding Partners ◽  
Secreted Proteases

Due to their capacity to process different proteins of the extracellular matrix (ECM), matrix metalloproteinases (MMPs) were initially described as a family of secreted proteases, functioning as main ECM regulators. However, through proteolytic processing of various biomolecules, MMPs also modulate intra- and extracellular pathways and networks. Thereby, they are functionally implicated in the regulation of multiple physiological and pathological processes. Consequently, MMP activity is tightly regulated through a combination of epigenetic, transcriptional, and post-transcriptional control of gene expression, proteolytic activation, post-translational modifications (PTMs), and extracellular inhibition. In addition, MMPs, their substrates and ECM binding partners are frequently modified by PTMs, which suggests an important role of PTMs in modulating the pleiotropic activities of these proteases. This review summarizes the recent progress towards understanding the role of PTMs (glycosylation, phosphorylation, glycosaminoglycans) on the activity of several members of the MMP family.

scholarly journals Improved Electrophoretic Separation to Assist the Monitoring of Bcl-xL Post-Translational Modifications

2019 ◽  
Vol 20 (22) ◽  
pp. 5571 ◽  
Author(s):  
Claude Bobo ◽  
Claire Céré ◽  
Mélody Dufossée ◽  
Alain Dautant ◽  
Violaine Moreau ◽  
...  
Keyword(s):  
Alkaline Treatment ◽  
Regulatory Mechanisms ◽  
Electrophoretic Separation ◽  
Survival Functions ◽  
Comprehensive Description ◽  
Post Translational Modifications ◽  
Gel Composition ◽  
Spontaneous Reaction

Bcl-xL is an oncogene of which the survival functions are finely tuned by post-translational modifications (PTM). Within the Bcl-2 family of proteins, Bcl-xL shows unique eligibility to deamidation, a time-related spontaneous reaction. Deamidation is still a largely overlooked PTM due to a lack of easy techniques to monitor Asn→Asp/IsoAsp conversions or Glu→Gln conversions. Being able to detect PTMs is essential to achieve a comprehensive description of all the regulatory mechanisms and functions a protein can carry out. Here, we report a gel composition improving the electrophoretic separation of deamidated forms of Bcl-xL generated either by mutagenesis or by alkaline treatment. Importantly, this new gel formulation proved efficient to provide the long-sought evidence that even doubly-deamidated Bcl-xL remains eligible for regulation by phosphorylation.

scholarly journals Inhibition of Transcription Induces Phosphorylation of YB-1 at Ser102 and Its Accumulation in the Nucleus

Cells ◽  
2019 ◽  
Vol 9 (1) ◽  
pp. 104 ◽  
Author(s):  
Dmitry A. Kretov ◽  
Daria A. Mordovkina ◽  
Irina A. Eliseeva ◽  
Dmitry N. Lyabin ◽  
Dmitry N. Polyakov ◽  
...  
Keyword(s):  
Gene Expression ◽  
Rna Polymerase Ii ◽  
Nuclear Localization ◽  
Kinase Activity ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Regulatory Mechanisms ◽  
Nuclear Accumulation ◽  
Nuclear Retention ◽  
Post Translational Modifications

The Y-box binding protein 1 (YB-1) is an RNA/DNA-binding protein regulating gene expression in the cytoplasm and the nucleus. Although mostly cytoplasmic, YB-1 accumulates in the nucleus under stress conditions. Its nuclear localization is associated with aggressiveness and multidrug resistance of cancer cells, which makes the understanding of the regulatory mechanisms of YB-1 subcellular distribution essential. Here, we report that inhibition of RNA polymerase II (RNAPII) activity results in the nuclear accumulation of YB-1 accompanied by its phosphorylation at Ser102. The inhibition of kinase activity reduces YB-1 phosphorylation and its accumulation in the nucleus. The presence of RNA in the nucleus is shown to be required for the nuclear retention of YB-1. Thus, the subcellular localization of YB-1 depends on its post-translational modifications (PTMs) and intracellular RNA distribution.

scholarly journals Trans-tail regulation-mediated suppression of cryptic transcription

2021 ◽  
Author(s):  
Jungmin Choi ◽  
Zae Young Ryoo ◽  
Dong-Hyung Cho ◽  
Hyun-Shik Lee ◽  
Hong-Yeoul Ryu
Keyword(s):  
Gene Expression ◽  
Rna Polymerase Ii ◽  
Histone Deacetylases ◽  
Transcriptional Control ◽  
Molecular Techniques ◽  
Transcriptional Elongation ◽  
Post Translational Modifications ◽  
Phosphorylation Pattern ◽  
Cryptic Transcription ◽  
H3k79 Methylation

AbstractCrosstalk between post-translational modifications of histone proteins influences the regulation of chromatin structure and gene expression. Among such crosstalk pathways, the best-characterized example is H2B monoubiquitination-mediated H3K4 and H3K79 methylation, which is referred to as trans-tail regulation. Although many studies have investigated the fragmentary effects of this pathway on silencing and transcription, its ultimate contribution to transcriptional control has remained unclear. Recent advances in molecular techniques and genomics have, however, revealed that the trans-tail crosstalk is linked to a more diverse cascade of histone modifications and has various functions in cotranscriptional processes. Furthermore, H2B monoubiquitination sequentially facilitates H3K4 dimethylation and histone sumoylation, thereby providing a binding platform for recruiting Set3 complex proteins, including two histone deacetylases, to restrict cryptic transcription from gene bodies. The removal of both ubiquitin and SUMO, small ubiquitin-like modifier, modifications from histones also facilitates a change in the phosphorylation pattern of the RNA polymerase II C-terminal domain that is required for subsequent transcriptional elongation. Therefore, this review describes recent findings regarding trans-tail regulation-driven processes to elaborate on their contribution to maintaining transcriptional fidelity.

The regulation of sarco(endo)plasmic reticulum calcium-ATPases (SERCA)

2015 ◽  
Vol 93 (10) ◽  
pp. 843-854 ◽  
Author(s):  
Andrew N. Stammers ◽  
Shanel E. Susser ◽  
Naomi C. Hamm ◽  
Michael W. Hlynsky ◽  
Dustin E. Kimber ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cardiac Tissue ◽  
Muscular Contraction ◽  
Regulatory Mechanisms ◽  
Post Translational Modifications ◽  
Disease States ◽  
Calcium Atpases ◽  
Plasmic Reticulum ◽  
Endogenous Proteins ◽  
Fast Twitch

The sarco(endo)plasmic reticulum calcium ATPase (SERCA) is responsible for transporting calcium (Ca2+) from the cytosol into the lumen of the sarcoplasmic reticulum (SR) following muscular contraction. The Ca2+ sequestering activity of SERCA facilitates muscular relaxation in both cardiac and skeletal muscle. There are more than 10 distinct isoforms of SERCA expressed in different tissues. SERCA2a is the primary isoform expressed in cardiac tissue, whereas SERCA1a is the predominant isoform expressed in fast-twitch skeletal muscle. The Ca2+ sequestering activity of SERCA is regulated at the level of protein content and is further modified by the endogenous proteins phospholamban (PLN) and sarcolipin (SLN). Additionally, several novel mechanisms, including post-translational modifications and microRNAs (miRNAs) are emerging as integral regulators of Ca2+ transport activity. These regulatory mechanisms are clinically relevant, as dysregulated SERCA function has been implicated in the pathology of several disease states, including heart failure. Currently, several clinical trials are underway that utilize novel therapeutic approaches to restore SERCA2a activity in humans. The purpose of this review is to examine the regulatory mechanisms of the SERCA pump, with a particular emphasis on the influence of exercise in preventing the pathological conditions associated with impaired SERCA function.

Histone post-translational modifications induced by histone deacetylase inhibition in transcriptional control units of NIS gene

2014 ◽  
Vol 41 (8) ◽  
pp. 5257-5265 ◽  
Author(s):  
Federica Baldan ◽  
Elisa Lavarone ◽  
Carla Di Loreto ◽  
Sebastiano Filetti ◽  
Diego Russo ◽  
...  
Keyword(s):  
Histone Deacetylase ◽  
Transcriptional Control ◽  
Post Translational Modifications ◽  
Histone Deacetylase Inhibition ◽  
Control Units ◽  
Nis Gene
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