Posttranslational regulation of CALHM1/3 channel: N ‐linked glycosylation and S ‐palmitoylation

2021 ◽  
Vol 35 (5) ◽  
Author(s):  
Motoki Okui ◽  
Tatsuro Murakami ◽  
Hongxin Sun ◽  
Chiaki Ikeshita ◽  
Narisato Kanamura ◽  
...  
Keyword(s):  
Posttranslational Regulation

Posttranslational Regulation of O6-Methylguanine-DNA Methyltransferase (MGMT) and New Opportunities for Treatment of Brain Cancers

2016 ◽  
Vol 16 (6) ◽  
pp. 455-464 ◽  
Author(s):  
Kalkunte S. Srivenugopal ◽  
Amit Rawat ◽  
Suryakant K. Niture ◽  
Ameya Paranjpe ◽  
Chinavenmani Velu ◽  
...  
Keyword(s):  
Dna Methyltransferase ◽  
Posttranslational Regulation ◽  
Methylguanine Dna Methyltransferase

Posttranslational Regulation of Bim by Caspase-3

2007 ◽  
Vol 1116 (1) ◽  
pp. 271-280 ◽  
Author(s):  
H. WAKEYAMA ◽  
T. AKIYAMA ◽  
Y. KADONO ◽  
M. NAKAMURA ◽  
Y. OSHIMA ◽  
...  
Keyword(s):  
Caspase 3 ◽  
Posttranslational Regulation

scholarly journals Fine-tuning autophagy: from transcriptional to posttranslational regulation

2016 ◽  
Vol 311 (3) ◽  
pp. C351-C362 ◽  
Author(s):  
Joëlle Botti-Millet ◽  
Anna Chiara Nascimbeni ◽  
Nicolas Dupont ◽  
Etienne Morel ◽  
Patrice Codogno
Keyword(s):  
Posttranslational Modifications ◽  
Inflammatory Responses ◽  
Chronic Inflammatory Disease ◽  
Autophagic Vacuole ◽  
Tissue Homeostasis ◽  
Fine Tuning ◽  
Eukaryotic Cells ◽  
Posttranslational Regulation ◽  
Atg Proteins ◽  
Diabetes And Obesity

Macroautophagy (hereafter called autophagy) is a vacuolar lysosomal pathway for degradation of intracellular material in eukaryotic cells. Autophagy plays crucial roles in tissue homeostasis, in adaptation to stress situations, and in immune and inflammatory responses. Alteration of autophagy is associated with cancer, diabetes and obesity, cardiovascular disease, neurodegenerative disease, autoimmune disease, infection, and chronic inflammatory disease. Autophagy is controlled by autophagy-related (ATG) proteins that act in a coordinated manner to build up the initial autophagic vacuole named the autophagosome. It is now known that the activities of ATG proteins are modulated by posttranslational modifications such as phosphorylation, ubiquitination, and acetylation. Moreover, transcriptional and epigenetic controls are involved in the regulation of autophagy in stress situations. Here we summarize and discuss how posttranslational modifications and transcriptional and epigenetic controls regulate the involvement of autophagy in the proteostasis network.

Constitutive RNA synthesis for the yeast activator ADR1 and identification of the ADR1-5c mutation: implications in posttranslational control of ADR1

1986 ◽  
Vol 6 (11) ◽  
pp. 4026-4030
Author(s):  
C L Denis ◽  
C Gallo
Keyword(s):  
Rna Synthesis ◽  
Potential Role ◽  
Glucose Repression ◽  
Posttranslational Regulation ◽  
Mrna Levels ◽  
Recognition Sequence ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Kinase Phosphorylation

The regulation of mRNA production for the yeast positive activator ADR1, a gene required for the expression of the glucose-repressible alcohol dehydrogenase (ADH II), was studied. ADR1 mRNA levels did not vary when yeasts were switched from glucose- to ethanol-containing medium, while ADH II expression increased 100-fold. The mRNA for the ADR1-5c allele, which augments ADH II expression 60-fold during glucose repression, was not present in greater abundance than ADR1 mRNA. Additionally, the ccr1-1 allele, which blocks ADH2 mRNA formation and partially suppresses the ADR1-5c phenotype, did not alter the levels of ADR1 mRNA. These results indicate that ADR1 is not transcriptionally controlled. To determine the character of the ADR1-5c mutation, the region containing the mutation was identified and sequenced. At base pair +683 a G-to-A transition was detected in the ADR1 coding sequence which would result in the substitution of a lysine residue for an arginine at amino acid 228. The location of the ADR1-5c mutation in the interior of the ADR1 coding sequences suggests that it enhances the activity of an extant but inactive ADR1 protein rather than increases the abundance of ADR1 by altered translation of its mRNA. The ADR1-5c mutation occurs in a region of the polypeptide corresponding to a cyclic AMP-dependent protein kinase phosphorylation recognition sequence. The potential role of reversible phosphorylation in the posttranslational regulation of ADR1 is discussed.

Herpesvirus-mediated stabilization of ICP0 expression neutralizes restriction by TRIM23

2021 ◽  
Vol 118 (51) ◽  
pp. e2113060118
Author(s):  
Xing Liu ◽  
Dhiraj Acharya ◽  
Eric Krawczyk ◽  
Chase Kangas ◽  
Michaela U. Gack ◽  
...  
Keyword(s):  
Viral Replication ◽  
Viral Gene Expression ◽  
Proteasomal Degradation ◽  
Viral Gene ◽  
Posttranslational Regulation ◽  
Early Proteins ◽  
Immediate Early Proteins ◽  
Simplex Virus ◽  
Functional Analyses ◽  
Hsv 1

Herpes simplex virus (HSV) infection relies on immediate early proteins that initiate viral replication. Among them, ICP0 is known, for many years, to facilitate the onset of viral gene expression and reactivation from latency. However, how ICP0 itself is regulated remains elusive. Through genetic analyses, we identify that the viral γ134.5 protein, an HSV virulence factor, interacts with and prevents ICP0 from proteasomal degradation. Furthermore, we show that the host E3 ligase TRIM23, recently shown to restrict the replication of HSV-1 (and certain other viruses) by inducing autophagy, triggers the proteasomal degradation of ICP0 via K11- and K48-linked ubiquitination. Functional analyses reveal that the γ134.5 protein binds to and inactivates TRIM23 through blockade of K27-linked TRIM23 autoubiquitination. Deletion of γ134.5 or ICP0 in a recombinant HSV-1 impairs viral replication, whereas ablation of TRIM23 markedly rescues viral growth. Herein, we show that TRIM23, apart from its role in autophagy-mediated HSV-1 restriction, down-regulates ICP0, whereas viral γ134.5 functions to disable TRIM23. Together, these results demonstrate that posttranslational regulation of ICP0 by virus and host factors determines the outcome of HSV-1 infection.

Mutagenesis and More: umuDC and the Escherichia coli SOS Response

Genetics ◽  
1998 ◽  
Vol 148 (4) ◽  
pp. 1599-1610 ◽  
Author(s):  
Bradley T Smith ◽  
Graham C Walker
Keyword(s):  
Escherichia Coli ◽  
Dna Damage ◽  
Cellular Response ◽  
Sos Response ◽  
Posttranslational Regulation ◽  
E Coli ◽  
Sos Mutagenesis ◽  
Induced Mutagenesis ◽  
Mechanistic Basis ◽  
Increase Cell Survival

Abstract The cellular response to DNA damage that has been most extensively studied is the SOS response of Escherichia coli. Analyses of the SOS response have led to new insights into the transcriptional and posttranslational regulation of processes that increase cell survival after DNA damage as well as insights into DNA-damage-induced mutagenesis, i.e., SOS mutagenesis. SOS mutagenesis requires the recA and umuDC gene products and has as its mechanistic basis the alteration of DNA polymerase III such that it becomes capable of replicating DNA containing miscoding and noncoding lesions. Ongoing investigations of the mechanisms underlying SOS mutagenesis, as well as recent observations suggesting that the umuDC operon may have a role in the regulation of the E. coli cell cycle after DNA damage has occurred, are discussed.

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