Alternative Splicing as a Mechanism for Regulating 14-3-3 Binding: Interactions between hD53 (TPD52L1) and 14-3-3 Proteins

Boutros, Rose; Bailey, Angela M.; Wilson, Samuel H.; Byrne, Jennifer A.

doi:10.1016/s0022-2836(03)00944-6

Cited by 37 publications

(72 citation statements)

References 44 publications

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“…7A). 28 To identify the ATM interaction domain within TPD52, pull-down assays were performed using a series of thioredoxin-6His-tagged truncated Tpd52 proteins (Fig. 7B).…”

Section: Tpd52 Directly Interacted With Atmmentioning

confidence: 99%

“…Western blot analyses and antibodies Cells were lysed in 3% SDS lysis buffer as described previously 28 or in NETN lysis buffer (150 mM NaCl, 5 mM EDTA, 50 mM Tris⋅HCl pH 7.5, 0.5% [v/v] Nonidet P-40) containing phosphatase and protease inhibitors (50 mM sodium fluoride, 1 mM sodium orthovanadate, 1 mM phenylmethylsulfonyl fluoride (PMSF), and EDTA-free Protease Inhibitor Cocktail Tablets from Roche Applied Science). 68 Between 30-60 μg total protein were resolved by SDS-PAGE on 12.5% mini polyacrylamide gels, 6% large polyacrylamide gels, or gradient NuPAGE ® Novex 4-12% Bis-Tris or NuPAGE ® Novex 3-8% Tris-Acetate gels (Life Technologies).…”

Section: Indirect Immunofluorescence Analyses and Quantitation Of γH2mentioning

confidence: 99%

“…TPD52 transcript and protein levels show wide variations in breast cancer samples and cell lines, 17,28,47 and as a gene amplification target, TPD52 has been predicted to acquire oncogenic functions through overexpression. Our data here further support this prediction, with TPD52 reducing ATM levels in cell lines with varying TPD52 levels.…”

mentioning

confidence: 99%

“…Similarly, exogenous TPD52 levels achieved in the 3T3 cell lines employed in this study were comparable with those detected in MCF-7 breast cancer cells, 17 which show moderate TPD52 levels. 28 That variations in TPD52 levels in normal cells may also be significant is suggested by associations between increased TPD52 expression and radiosensitivity in independent studies using lymphocytes 23 or lymphoblastoid cell lines, 24 indicating that variations in TPD52 levels could also alter radiosensitivity in normal cells.…”

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Tumor protein D52 represents a negative regulator of ATM protein levels

et al. 2013

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“…7A). 28 To identify the ATM interaction domain within TPD52, pull-down assays were performed using a series of thioredoxin-6His-tagged truncated Tpd52 proteins (Fig. 7B).…”

Section: Tpd52 Directly Interacted With Atmmentioning

confidence: 99%

Section: Indirect Immunofluorescence Analyses and Quantitation Of γH2mentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Tumor protein D52 represents a negative regulator of ATM protein levels

et al. 2013

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“…This possible role of hD53L1 as an inhibitor of ASK1-inhibiting proteins may explain why the kinase activity of ASK1 is not induced significantly. Whereas little is known of hD52 family protein function, a recent report that hD53 (TPD 52L1) and hD54 (TPD52L2) contain 14-3-3 binding motifs suggests possible roles of hD52 family members in 14-3-3-regulated cellular processes (45). However, the fact that hD52 and hD53L1 lack 14-3-3 binding motifs indicates that there are functional differences among D52 family proteins in modulating cellular processes.…”

Section: Discussionmentioning

confidence: 99%

Positive Regulation of Apoptosis Signal-regulating Kinase 1 by hD53L1

Cho

Kim

et al. 2004

Journal of Biological Chemistry

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Apoptosis signal-regulating kinase 1 (ASK1) is a mitogen-activated protein kinase kinase kinase family member that plays a central role in cytokine-and stressinduced apoptosis by activating c-Jun N-terminal kinase and p38 signaling cascades. ASK1-induced apoptotic activity is up-regulated by two cellular factors, Daxx and TRAF2, through direct protein-protein interactions. Daxx and TRAF2 are death receptor-associated proteins in Fas and tumor necrosis factor-␣ pathways, respectively. Recent studies suggest that calcium signaling may regulate ASK1 pathway. Here we report that human D53L1, a member of the tumor protein D52 family involved in cell proliferation and calcium signaling, up-regulates the ASK1-induced apoptosis. The human D53L1 physically interacts with the C-terminal regulatory domain of ASK1 and promotes ASK1-induced apoptotic activity by activating caspase signaling in mammalian cells. In luciferase reporter assays, hD53L1 activates c-Jun N-terminal kinase-mediated transactivation in the presence of ASK1. Expression of hD53L1 enhances autophosphorylation and kinase activity of ASK1 but has no effect on ASK1 oligomerization that is necessary for kinase activity and on binding of ASK1 to MKK6, a downstream factor of ASK1. Taken together, these results suggest that activation of ASK1 by hD53L1 may provide a novel mechanism for ASK1 regulation.

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Tumor protein D52 (TPD52) is overexpressed and a gene amplification target in ovarian cancer

Byrne

Balleine

Fejzo

et al. 2005

Intl Journal of Cancer

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Recurrent chromosome 8q gain in ovarian carcinoma is likely to reflect the existence of multiple target loci, as the separate gain of chromosome bands 8q21 and 8q24 has been reported in independent studies. Since tumor protein D52 (TPD52) has been identified as a chromosome 8q21 amplification target in breast and prostate carcinoma, we compared TPD52 expression in normal ovarian epithelium (n 5 9), benign serous adenomas (n 5 11), serous borderline tumors (n 5 6) and invasive carcinomas of the major histologic subtypes (n 5 57) using immunohistochemistry. These analyses revealed that all normal ovarian epithelium samples and benign serous tumors were predominantly TPD52-negative, whereas TPD52 was overexpressed in most (44/57; 77%) ovarian carcinomas regardless of histologic subtype. TPD52 subcellular localization was predominantly cytoplasmic, although nuclear localization was also frequently observed in mucinous and clear cell carcinomas. In an independent cohort of stage III serous carcinomas (n 5 18), we also directly compared in situ TPD52 expression using immunohistochemistry and TPD52 copy number using interphase FISH analyses. This revealed that TPD52 dosage and TPD52 expression were significantly positively correlated. TPD52 therefore represents a novel molecular marker in ovarian cancer, which is broadly expressed across the different histologic subtypes and whose upregulation frequently reflects increased TPD52 copy number. ' 2005 Wiley-Liss, Inc.

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Alternative Splicing as a Mechanism for Regulating 14-3-3 Binding: Interactions between hD53 (TPD52L1) and 14-3-3 Proteins

Cited by 37 publications

References 44 publications

Tumor protein D52 represents a negative regulator of ATM protein levels

Tumor protein D52 represents a negative regulator of ATM protein levels

Positive Regulation of Apoptosis Signal-regulating Kinase 1 by hD53L1

Tumor protein D52 (TPD52) is overexpressed and a gene amplification target in ovarian cancer

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