Evidence That Phospholipase δ1 Is the Effector in the Gh (Transglutaminase II)-mediated Signaling

Feng, Jingyuan; Rhee, Sue Goo; Im, Mie‐Jae

doi:10.1074/jbc.271.28.16451

Cited by 175 publications

(173 citation statements)

References 27 publications

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“…Tissue transglutaminase has been proposed to be implicated in a vast array of cellular processes, including the suppression of cell proliferation, differentiation, and signal transduction (30)(31)(32)(33)(34).…”

Section: Discussionmentioning

confidence: 99%

An Autocrine Loop Involving Ret and Glial Cell–Derived Neurotrophic Factor Mediates Retinoic Acid–Induced Neuroblastoma Cell Differentiation

Cerchia

D’Alessio

Amabile

et al. 2006

Molecular Cancer Research

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Section: Discussionmentioning

confidence: 99%

An Autocrine Loop Involving Ret and Glial Cell–Derived Neurotrophic Factor Mediates Retinoic Acid–Induced Neuroblastoma Cell Differentiation

Cerchia

D’Alessio

Amabile

et al. 2006

Molecular Cancer Research

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“…GTP-bound TGase participates in signaling pathways that link cell surface receptors to intracellular effectors. The most studied example of this involved the up-regulation of phospholipase C activity by the ␣ 1 -adrenergic receptor (13,14), where it was shown that the ␣ 1 -adrenergic receptor stimulated the GTP binding activity of TGase. The GTP-bound TGase species, in turn, was shown to stimulate phosphoinositide lipid hydrolysis by phospholipase C. The ability of TGase to transduce signals adds another dimension to its functionality and may help explain how the same protein can be linked to several, sometimes opposing, cellular responses.…”

mentioning

confidence: 99%

Activation of the Ras-ERK Pathway Inhibits Retinoic Acid-induced Stimulation of Tissue Transglutaminase Expression in NIH3T3 Cells

Antonyak

McNeill

Wakshlag

et al. 2003

Journal of Biological Chemistry

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Retinoic acid (RA) is a potent activator of tissue transglutaminase (TGase) expression, and it was recently shown that phosphoinositide 3-kinase (PI3K) activity was required for RA to increase TGase protein levels. To better understand how RA-mediated TGase expression is regulated, we considered whether co-stimulation of NIH3T3 cells with RA and epidermal growth factor (EGF), a known activator of PI3K, would facilitate the induction or increase the levels of TGase expression. Instead of enhancing these parameters, EGF inhibited RA-induced TGase expression. Activation of the Ras-ERK pathway by EGF was sufficient to elicit this effect, since continuous Ras signaling mimicked the actions of EGF and inhibited RA-induced TGase expression, whereas blocking ERK activity in these same cells restored the ability of RA to up-regulate TGase expression. However, TGase activity is not antagonistic to EGF signaling. The mitogenic and anti-apoptotic effects of EGF were not compromised by TGase overexpression, and in fact, exogenous TGase expression promoted basal cell growth and resistance to serum deprivation-induced apoptosis. Moreover, analysis of TGase expression and GTP binding activity in a number of cell lines revealed high basal TGase GTP binding activity in tumor cell lines U87 and MDAMB231, indicating that constitutively active TGase may be a characteristic of certain cancer cells. These findings demonstrate that TGase may serve as a survival factor and RA-induced TGase expression requires the activation of PI3K but is antagonized by the Ras-ERK pathway.

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“…PLC-␥s are regulated by receptor or nonreceptor protein-tyrosine kinases and PIP 3 (4). PLC-␦s are regulated by a GTP-binding protein transglutaminase (7). PLC-␦s are also more sensitive to Ca 2ϩ than the other isozymes and, unlike PLC-␥s and PLC-␤s, are activated by Ca 2ϩ alone (8).…”

mentioning

confidence: 99%

Reassembly of Phospholipase C-β2 from Separated Domains

Zhang

Neer

2001

Journal of Biological Chemistry

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Phosphatidylinositol-specific phospholipase C-␤s (PLC-␤s) are the only PLC isoforms that are regulated by G protein subunits. To further understand the regulation of PLC-␤ 2 by G proteins and the functional roles of PLC-␤ 2 structural domains, we tested whether the separately expressed amino and carboxyl halves of PLC-␤ 2 could associate to form catalytically active enzymes as two polypeptides, and we explored how the complexes thus formed would be regulated by G protein ␤␥ subunits (G␤␥). We expressed cDNA constructs encoding PLC-␤ 2 fragments of different lengths in COS-7 cells and demonstrated by coimmunoprecipitation that the coexpressed fragments could assemble and functionally reconstitute an active PLC-␤ 2 . The pleckstrin homology domain of PLC-␤ 2 was required for its targeting to the membrane and for substrate hydrolysis. Reconstituted enzymes that contained the linker region that joins the two catalytic domains were as active or more active than the wild-type PLC-␤ 2 . When the linker region was removed, basal PLC-␤ 2 enzymatic activity was increased further, suggesting that the linker region exerts an inhibitory effect on basal PLC-␤ 2 activity. The reconstituted enzymes, like wild-type PLC-␤ 2 , were activated by G␤␥; when the C-terminal region was present in these constructs, they were also activated by G␣ q . G␤␥ and G␣ q activated these PLC-␤ 2 constructs equally in the presence or absence of the linker region. We conclude that the linker region is an inhibitory element in PLC-␤ 2 and that G␤␥ and G␣ q do not stimulate PLC-␤ 2 through easing the inhibition of enzymatic activity by the linker region.Phosphatidylinositol-specific phospholipase Cs (PLCs) 1 are enzymes that catalyze the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP 2 ) to generate two second messengers, inositol 1,4,5-trisphosphate (IP 3 ) and diacylglycerol. IP 3 releases Ca 2ϩ from intracellular stores, and diacylglycerol activates protein kinase C (for review see Refs.

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Evidence That Phospholipase δ1 Is the Effector in the Gh (Transglutaminase II)-mediated Signaling

Cited by 175 publications

References 27 publications

An Autocrine Loop Involving Ret and Glial Cell–Derived Neurotrophic Factor Mediates Retinoic Acid–Induced Neuroblastoma Cell Differentiation

An Autocrine Loop Involving Ret and Glial Cell–Derived Neurotrophic Factor Mediates Retinoic Acid–Induced Neuroblastoma Cell Differentiation

Activation of the Ras-ERK Pathway Inhibits Retinoic Acid-induced Stimulation of Tissue Transglutaminase Expression in NIH3T3 Cells

Reassembly of Phospholipase C-β2 from Separated Domains

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