Differential Phosphorylation of c-Jun and JunD in Response to the Epidermal Growth Factor Is Determined by the Structure of MAPK Targeting Sequences

Vinciguerra, Maria; Vivacqua, Adele; Fasanella, Giovanna; Gallo, Adriana; Cuozzo, Concetta; Morano, Annalisa; Maggiolini, Marcello; Musti, Anna Maria

doi:10.1074/jbc.m308721200

Cited by 46 publications

(44 citation statements)

References 31 publications

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“…14,20 JunD is phosphorylated at Ser100 in activated HSCs and is necessary for stimulation of TIMP-1 gene transcription. We propose that Ser100 phosphorylated JunD homodimers operate in concert with either RUNX1A or RUNX2 to generate high-level TIMP-1 expression by activated HSCs.…”

Section: Discussionmentioning

confidence: 99%

“…The Ser100 of JunD is also an efficient target for phosphorylation by ERK1/2. 14,20 Treatment of rat HSCs with the ERK1/2 inhibitor PD98059 resulted in 40% repression of TIMP-1 promoter activity but had no effect on promoter activity in 3T3 cells (Fig. 7C).…”

Section: Serine Phosphorylation Of Jund Is Required For Transactivatimentioning

confidence: 99%

“…18,19 The N-terminus of JunD contains 3 MAPK-regulated phospho-acceptor sites (Ser90, Ser100, and Thr117) that are phosphorylated in response to ERK1/2 and JNK activation. 14,20 To determine if HSCs support phosphorylation of JunD, human LX-2 HSCs were transfected with the JunD expression vector. JunD-transfected LX-2 HSCs expressed 2 major protein species (39 and 43 kDa) reactive with both anti-phosphoJun and anti-JunD (Fig.…”

Section: Serine Phosphorylation Of Jund Is Required For Transactivatimentioning

confidence: 99%

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JunD is a profibrogenic transcription factor regulated by Jun N-terminal kinase-independent phosphorylation

et al. 2006

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A ctivated (or myofibroblastic) hepatic stellate cells (HSCs) are cellular mediators of liver fibrosis through their secretion of interstitial collagens and tissue inhibitor of metalloproteinase-1 (TIMP-1), 1,2 which is a broad specific inhibitor of the matrix metalloproteinases (MMPs) and prevents MMP-catalyzed degradation of interstitial collagens in order to promote collagen deposition. A second fibrogenic role identified for TIMP-1 is as a suppressor of HSC apoptosis. 3 TIMP-1 gene transcription is induced during culture activation of isolated HSCs and is under the control of regulatory elements in the TIMP-1 promoter including activator protein-1 (AP-1) and RUNX binding sites. [4][5][6][7]

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Section: Discussionmentioning

confidence: 99%

Section: Serine Phosphorylation Of Jund Is Required For Transactivatimentioning

confidence: 99%

Section: Serine Phosphorylation Of Jund Is Required For Transactivatimentioning

confidence: 99%

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JunD is a profibrogenic transcription factor regulated by Jun N-terminal kinase-independent phosphorylation

et al. 2006

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“…The function and regulation of the subunits of the AP-1 complex are influenced by their intra-molecular interactions (van Dam and Castellazzi, 2001;Vogt, 2002) and their response to other cellular proteins (Vinciguerra et al, 2004). JunB and JunD differ from c-Jun in their DNA-binding and dimerization domains and affinities (Ryseck and Bravo, 1991;Deng and Karin, 1993).…”

Section: Introductionmentioning

confidence: 99%

TAp63α indirectly regulates a cutaneous HPV promoter through complex formation with Jun family members

et al. 2006

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“…JNKs also phosphorylate and activate JunD and ATF-2 (45,46). By contrast, the kinases that regulate the activity of Fos proteins are not yet well characterized, although a plethora of candidates have been suggested (47)(48)(49).…”

Section: Genetics and Epigenetics In Respiratory Epithelium Carcinogementioning

confidence: 99%

The Activator Protein-1 Transcription Factor in Respiratory Epithelium Carcinogenesis

Karamouzis

Konstantinopoulos²,

Papavassiliou³

2007

Molecular Cancer Research

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Respiratory epithelium cancers are the leading cause of cancer-related death worldwide. The multistep natural history of carcinogenesis can be considered as a gradual accumulation of genetic and epigenetic aberrations, resulting in the deregulation of cellular homeostasis. Growing evidence suggests that crosstalk between membrane and nuclear receptor signaling pathways along with the activator protein-1 (AP-1) cascade and its cofactor network represent a pivotal molecular circuitry participating directly or indirectly in respiratory epithelium carcinogenesis. The crucial role of AP-1 transcription factor renders it an appealing target of future nuclear-directed anticancer therapeutic and chemoprevention approaches. In the present review, we will summarize the current knowledge regarding the implication of AP-1 proteins in respiratory epithelium carcinogenesis, highlight the ongoing research, and consider the future perspectives of their potential therapeutic interest. (Mol Cancer Res 2007;5(2):109 -20)

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Differential Phosphorylation of c-Jun and JunD in Response to the Epidermal Growth Factor Is Determined by the Structure of MAPK Targeting Sequences

Abstract: MAPK phosphorylation of various substrates is medi-

Cited by 46 publications

References 31 publications

JunD is a profibrogenic transcription factor regulated by Jun N-terminal kinase-independent phosphorylation

JunD is a profibrogenic transcription factor regulated by Jun N-terminal kinase-independent phosphorylation

TAp63α indirectly regulates a cutaneous HPV promoter through complex formation with Jun family members

The Activator Protein-1 Transcription Factor in Respiratory Epithelium Carcinogenesis

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