ADP-Ribosylation of Tubulin by Chicken NAD-Arginine ADP-Ribosyltransferase Suppresses Microtubule Formation.

Terashima, Masaharu; Yamamori, Chikako; Tsuchiya, Masaharu; Shimoyama, Makoto

doi:10.3177/jnsv.45.393

Cited by 5 publications

(4 citation statements)

References 23 publications

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“…SIRT2, a predominantly cytoplasmic protein associated with microtubules and acting as a bona fide tubulin deacetylase (289), could be responsible for the arginine-specific mono-ADP-ribosylation of both alpha and beta chains of tubulin. Several studies provided evidence that both deacetylation and arginine-specific mono-ADP-ribosylation of tubulins are involved in depolymerization of the microtubules (260,289,351,403). The heterotrimeric GTP-binding proteins and small GTPases may represent substrates for the predominantly cytoplasmic members of the Pl-MART family ( Table 1).…”

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confidence: 99%

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

Hassa

Haenni

Elser

et al. 2006

Microbiol Mol Biol Rev

635

644

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SUMMARY Since poly-ADP ribose was discovered over 40 years ago, there has been significant progress in research into the biology of mono- and poly-ADP-ribosylation reactions. During the last decade, it became clear that ADP-ribosylation reactions play important roles in a wide range of physiological and pathophysiological processes, including inter- and intracellular signaling, transcriptional regulation, DNA repair pathways and maintenance of genomic stability, telomere dynamics, cell differentiation and proliferation, and necrosis and apoptosis. ADP-ribosylation reactions are phylogenetically ancient and can be classified into four major groups: mono-ADP-ribosylation, poly-ADP-ribosylation, ADP-ribose cyclization, and formation of O-acetyl-ADP-ribose. In the human genome, more than 30 different genes coding for enzymes associated with distinct ADP-ribosylation activities have been identified. This review highlights the recent advances in the rapidly growing field of nuclear mono-ADP-ribosylation and poly-ADP-ribosylation reactions and the distinct ADP-ribosylating enzyme families involved in these processes, including the proposed family of novel poly-ADP-ribose polymerase-like mono-ADP-ribose transferases and the potential mono-ADP-ribosylation activities of the sirtuin family of NAD+-dependent histone deacetylases. A special focus is placed on the known roles of distinct mono- and poly-ADP-ribosylation reactions in physiological processes, such as mitosis, cellular differentiation and proliferation, telomere dynamics, and aging, as well as “programmed necrosis” (i.e., high-mobility-group protein B1 release) and apoptosis (i.e., apoptosis-inducing factor shuttling). The proposed molecular mechanisms involved in these processes, such as signaling, chromatin modification (i.e., “histone code”), and remodeling of chromatin structure (i.e., DNA damage response, transcriptional regulation, and insulator function), are described. A potential cross talk between nuclear ADP-ribosylation processes and other NAD+-dependent pathways is discussed.

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confidence: 99%

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

Hassa

Haenni

Elser

et al. 2006

Microbiol Mol Biol Rev

635

644

View full text Add to dashboard Cite

show abstract

“…The tissue distribution also varies among species; Arts are found in muscle, heart, spleen, brain, Tcells and polymorphonuclear leucocytes [4][5][6][7][11][12][13]18,19]. The putative roles of ADP-ribosylation include functional changes via modification of many target proteins, including guaninenucleotide-binding protein, actin, integrin, fibronectin and some physiologically active peptides [9,10,[32][33][34][35][36][37][38][39]. There are at least two forms of Arts, i.e.…”

Section: Discussionmentioning

confidence: 99%

Purification, characterization and molecular cloning of glycosylphosphatidylinositol-anchored arginine-specific ADP-ribosyltransferases from chicken

Terashima

Osago

Hara

et al. 2005

Biochemical Journal

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Mono-ADP-ribosylation is a post-translational modification that regulates the functions of target proteins or peptides by attaching an ADP-ribose moiety. Here we report the purification, molecular cloning, characterization and tissue-specific distribution of novel arginine-specific Arts (ADP-ribosyltransferases) from chicken. Arts were detected in various chicken tissues as GPI (glycosylphosphatidylinositol)-anchored forms, and purified from the lung membrane fraction. By molecular cloning based on the partial amino acid sequence using 5'- and 3'-RACE (rapid amplification of cDNA ends), two full-length cDNAs of chicken GPI-anchored Arts, cgArt1 (chicken GPI-anchored Art1) and cgArt2, were obtained. The cDNA of cgArt1 encoded a novel polypeptide of 298 amino acids which shows a high degree of identity with cgArt2 (82.9%), Art6.1 (50.2%) and rabbit Art1 (42.1%). In contrast, the nucleotide sequence of cgArt2 was identical with that of Art7 cloned previously from chicken erythroblasts. cgArt1 and cgArt2 proteins expressed in DT40 cells were shown to be GPI-anchored Arts with a molecular mass of 45 kDa, and these Arts showed different enzymatic properties from the soluble chicken Art, Art6.1. RNase protection assays and real-time quantitative PCR revealed distinct expression patterns of the two Arts; cgArt1 was expressed predominantly in the lung, spleen and bone marrow, followed by the heart, kidney and muscle, while cgArt2 was expressed only in the heart and skeletal muscle. Thus GPI-anchored Arts encoded by the genes cgArt1 and cgArt2 are expressed extensively in chicken tissues. It may be worthwhile determining the functional roles of ADP-ribosylation in each tissue.

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“…Subsequently endogenous mammalian mono (ADP-ribosyl) transferases were characterized as a family of enzymes that are related to bacterial toxins [4,5]. These enzymes include ecto-ADP-ribose transferases (ecto-ARTs) and a few intracellular enzymes which could catalysis mono-ADP-ribosylation but with almost undefined structure [6,7,8,9,10,11,12,13]. The ecto-ARTs include seven members, designated as ART1 through ART7.…”

Section: Introductionmentioning

confidence: 99%

ART1 Silencing Enhances Apoptosis of Mouse CT26 Cells via the PI3K/Akt/NF-κB Pathway

Xiao¹,

Wang²,

Yang³

et al. 2013

Cell Physiol Biochem

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Background/Aims: Colorectal carcinoma is one of the most common cancers world-wide, with high morbidity and mortality rates. Arginine ADP-ribosyltransferase 1(ART1) is an important ecto-ADP-ribose transferase and has been proven to be intimately involved in a number of biological processes. However, the influence of ART1 on survival and apoptosis of colorectal carcinoma cells and the potential mechanism of action of ART1 remain uncharacterized. Methods: ART1 was silenced via lentiviral vector-mediated short hairpin RNA (shRNA) in CT26 colon carcinoma cells, and cisplatin (CDDP) was applied to induce apoptosis. Survival and apoptosis rate of CT26 cells was assessed by CCK8 assay, flow cytometry and Hoechst 33342 staining. Expression and activity of signaling proteins were detected by Western blot. Results: ART1 knockdown enhanced the inhibition of cell survival and increased the apoptosis induced by CDDP. Furthermore, the reduced survival rate correlated with reduced levels of phos-Akt^Thr308 and phos-IκBa and reduced NF-κB p65 nuclear translocation. A decline in Bcl-2 and Bcl-xl expression and an increase in Bax expression may explain the enhanced apoptosis. Conclusion: This study provides a molecular mechanism for the function of ART1 in colorectal carcinoma and defines a potential therapeutic target for the enhanced treatment of this prominent world-wide disease.

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ADP-Ribosylation of Tubulin by Chicken NAD-Arginine ADP-Ribosyltransferase Suppresses Microtubule Formation.

Cited by 5 publications

References 23 publications

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

Purification, characterization and molecular cloning of glycosylphosphatidylinositol-anchored arginine-specific ADP-ribosyltransferases from chicken

ART1 Silencing Enhances Apoptosis of Mouse CT26 Cells via the PI3K/Akt/NF-κB Pathway

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ADP-Ribosylation of Tubulin by Chicken NAD-Arginine ADP-Ribosyltransferase Suppresses Microtubule Formation.

Cited by 5 publications

References 23 publications

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

Purification, characterization and molecular cloning of glycosylphosphatidylinositol-anchored arginine-specific ADP-ribosyltransferases from chicken

ART1 Silencing Enhances Apoptosis of Mouse CT26 Cells via the PI3K/Akt/NF-&#954;B Pathway

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ART1 Silencing Enhances Apoptosis of Mouse CT26 Cells via the PI3K/Akt/NF-κB Pathway