PLIP, a Novel Splice Variant of Tip60, Interacts with Group IV Cytosolic Phospholipase A<sub>2</sub>, Induces Apoptosis, and Potentiates Prostaglandin Production

Am, Sheridan; Force, Thomas; Yoon, Haesang; O’Leary, Eileen; Choukroun, Gabriel; Mr, Taheri; Jv, Bonventre

doi:10.1128/mcb.21.14.4470-4481.2001

Cited by 63 publications

(53 citation statements)

References 75 publications

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“…Subsequently, full-length Tip60 has been found in association with membrane-bound receptors in a study that verified both nuclear and cytoplasmic expression (Sliva et al, 1999). Recent studies suggest that Tip60 shuttles between the cytoplasm and the nucleus in response to stimuli such as endothelins (Lee et al, 2001) and serum starvation (Sheridan et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Expression of Tip60, an androgen receptor coactivator, and its role in prostate cancer development

et al. 2003

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Section: Introductionmentioning

confidence: 99%

Expression of Tip60, an androgen receptor coactivator, and its role in prostate cancer development

et al. 2003

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“…Second, cPLA 2 -interacting protein (PLIP), a splice variant of Tip60, interacts with the N-terminal region of cPLA 2 a. 72) In renal mesangial cells, cPLA 2 a colocalizes with PLIP in the nucleus. Despite this unusual cPLA 2 a localization, overexpression of PLIP potentiates cPLA 2 a-mediated PGE 2 production and serum deprivationassociated apoptosis.…”

Section: -5 Regulation By Protein Interaction and Cleavagementioning

confidence: 99%

Regulatory Mechanism and Physiological Role of Cytosolic Phospholipase A2

Hirabayashi

Murayama

Shimizu

2004

Biological & Pharmaceutical Bulletin

216

184

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Cytosolic phospholipase A 2 a a (cPLA 2 a a) preferentially hydrolyzes phospholipids containing arachidonic acid and plays a key role in the biosynthesis of eicosanoids. This review discusses the essential features of cPLA 2 a a regulation and addresses new insights into the functional properties of this enzyme. Full activation of the enzyme requires Ca 2؉ binding to an N-terminal C2 domain and phosphorylation on serine residues. Ca 2؉ binding induces translocation of cPLA 2 a a from the cytosol to the perinuclear membranes. Serine phosphorylation is mediated by mitogen-activated protein kinases (MAPKs), Ca 2؉ /calmodulin-dependent protein kinase II, and MAPK-interacting kinase Mnk1. Interaction with proteins and lipids, which include vimentin, annexins, NADPH oxidase, phosphatidylcholine, phosphatidylinositol 4,5-bisphosphate (PIP 2 ), and ceramide-1-phosphate, can also modulate the activity of cPLA 2 a a. Recent evidence has established the physiological and pathological roles of cPLA 2 a a using cPLA 2 a a knockout mice. This enzyme has been implicated in fertility, striated muscle growth, renal concentration, postischemic brain injury, arthritis, inflammatory bone resorption, intestinal polyposis, pulmonary fibrosis, acute respiratory distress syndrome, and autoimmune encephalomyelitis. Now novel three paralogs, cPLA 2 b b, cPLA 2 g g, and cPLA 2 d d, have been identified in humans. cPLA 2 g g is distinct from others in that it is farnesylated and lacks the C2 domain. Biological roles for these new enzymes have not yet been defined.

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“…The NuA4 complex itself is broadly conserved (Doyon and Côté, 2004) and the human catalytic subunit Tip60 functions in nontranscriptional components of apoptosis and signaling processes (Ikura et al, 2000;Sheridan et al, 2001). Tip60 has been linked to DNA repair (Ikura et al, 2000) and a role for Esa1p and the Yng2p NuA4 subunit was found in replication-coupled DNA double-stranded break repair (Bird et al, 2002;Choy and Kron, 2002).…”

Section: Introductionmentioning

confidence: 99%

“…Esa1p is the catalytic component of the 1.4-MDa NuA4 HAT complex that is important for transcriptional activation both in vitro and in vivo at specific target loci, including many ribosomal protein genes (reviewed in Doyon and Côté, 2004). Esa1p also functions in the highly active, smaller picNuA4 complex (Boudreault et al, 2003).The NuA4 complex itself is broadly conserved (Doyon and Côté, 2004) and the human catalytic subunit Tip60 functions in nontranscriptional components of apoptosis and signaling processes (Ikura et al, 2000;Sheridan et al, 2001). Tip60 has been linked to DNA repair (Ikura et al, 2000) and a role for Esa1p and the Yng2p NuA4 subunit was found in replication-coupled DNA double-stranded break repair (Bird et al, 2002;Choy and Kron, 2002).…”

mentioning

confidence: 99%

Distinct Roles for the Essential MYST Family HAT Esa1p in Transcriptional Silencing

Clarke

Samal

Pillus

2006

MBoC

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Among acetyltransferases, the MYST family enzyme Esa1p is distinguished for its essential function and contribution to transcriptional activation and DNA double-stranded break repair. Here we report that Esa1p also plays a key role in silencing RNA polymerase II (Pol II)-transcribed genes at telomeres and within the ribosomal DNA (rDNA) of the nucleolus. These effects are mediated through Esa1p's HAT activity and correlate with changes within the nucleolus. Esa1p is enriched within the rDNA, as is the NAD-dependent protein deacetylase Sir2p, and the acetylation levels of key Esa1p histone targets are reduced in the rDNA in esa1 mutants. Although mutants of both ESA1 and SIR2 have enhanced rates of rDNA recombination, esa1 effects are more modest yet result in distinct structural changes of rDNA chromatin. Surprisingly, increased expression of ESA1 can bypass the requirement for Sir2p in rDNA silencing, suggesting that these two enzymes with seemingly opposing activities both contribute to achieve optimal nucleolar chromatin structure and function. INTRODUCTIONHistone modifications such as phosphorylation, methylation, acetylation, and deacetylation provide a mechanism by which chromatin structure is modulated to affect gene expression both positively and negatively (for reviews see Strahl and Allis, 2000;Iizuka and Smith, 2003;Kurdistani and Grunstein, 2003). The acetylation of lysine residues on histone N-terminal tails is classically linked to increases in gene expression and more directly to roles in transcriptional activation. By contrast, deacetylation of histones is most frequently correlated with transcriptionally silent chromatin. As more is learned about the enzymes catalyzing these modifications, the histone acetyltransferases (HATs) and histone deacetylases (HDACs), simple functional distinctions between acetylation and deacetylation of histones do not hold (Iizuka and Smith, 2003). For example, in several organisms, mutations in RPD3, a gene encoding a deacetylase, lead to increases in silencing rather than the expected decreases (DeRubertis et al., 1996;Rundlett et al., 1996). This brings forward the possibility that histone acetylation may play an important part in both silent and active chromatin. In addition, coactivator proteins, such as the histone acetyltransferases p300 and CBP and nuclear hormone receptors, appear to have roles in transcriptional repression through acetylation and association with particular binding partners (for examples, see Chen and Li, 1998;Waltzer and Bienz, 1998;Baluchamy et al., 2003;Girdwood et al., 2003;Rajabi et al., 2005). Thus, understanding of multiple roles for acetylation in controlling gene expression is expanding.In Saccharomyces cerevisiae, there are three regions of the genome controlled by chromatin-mediated transcriptional silencing: telomeres, the silent mating-type loci HMR and HML, and the rDNA array. Many factors are important for transcriptional silencing at subsets of these loci including the four core histones, the repressor activator protein Rap1...

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PLIP, a Novel Splice Variant of Tip60, Interacts with Group IV Cytosolic Phospholipase A₂, Induces Apoptosis, and Potentiates Prostaglandin Production

Abstract: The group IV cytosolic phospholipase A 2 (cPLA 2 ) has been localized to the nucleus (M. R. Sierra-Honigmann, J. R. Bradley, and J. S. Pober, Lab. Investig. 74:684-695, 1996) and is known to translocate from the cytosolic compartment to the nuclear membrane (S. Glover, M.

Cited by 63 publications

References 75 publications

Expression of Tip60, an androgen receptor coactivator, and its role in prostate cancer development

Expression of Tip60, an androgen receptor coactivator, and its role in prostate cancer development

Regulatory Mechanism and Physiological Role of Cytosolic Phospholipase A2

Distinct Roles for the Essential MYST Family HAT Esa1p in Transcriptional Silencing

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PLIP, a Novel Splice Variant of Tip60, Interacts with Group IV Cytosolic Phospholipase A2, Induces Apoptosis, and Potentiates Prostaglandin Production

Abstract: The group IV cytosolic phospholipase A 2 (cPLA 2 ) has been localized to the nucleus (M. R. Sierra-Honigmann, J. R. Bradley, and J. S. Pober, Lab. Investig. 74:684-695, 1996) and is known to translocate from the cytosolic compartment to the nuclear membrane (S. Glover, M.

Cited by 63 publications

References 75 publications

Expression of Tip60, an androgen receptor coactivator, and its role in prostate cancer development

Expression of Tip60, an androgen receptor coactivator, and its role in prostate cancer development

Regulatory Mechanism and Physiological Role of Cytosolic Phospholipase A2

Distinct Roles for the Essential MYST Family HAT Esa1p in Transcriptional Silencing

Contact Info

Product

Resources

About

PLIP, a Novel Splice Variant of Tip60, Interacts with Group IV Cytosolic Phospholipase A₂, Induces Apoptosis, and Potentiates Prostaglandin Production