Laminar flow inhibits TNF-induced ASK1 activation by preventing dissociation of ASK1 from its inhibitor 14-3-3

Liu, Yingmei; Yin, Guoyong; Surapisitchat, James; Berk, Bradford C.; Wang, Min

doi:10.1172/jci11947

Cited by 107 publications

(125 citation statements)

References 37 publications

Supporting

Mentioning

115

Contrasting

Order By: Relevance

“…As a control, we also measured the phosphorylation of ASK1 at Ser-967 with a phosphospecific antibody, a critical site for ASK1 binding to 14-3-3. Consistent with reports from our and other laboratories (13,14,22,28), ASK1 was basally phosphorylated at Ser-967 (thus binding to 14-3-3) and H 2 O 2 induced dephosphorylation of ASK1 at Ser-967. However, Gö6976, but not Gö6983, prevented H 2 O 2 -induced dephosphorylation of ASK1 at pSer-967 (Fig.…”

Section: A Critical Role Of Pkd In Mediating H 2 O 2 -Induced Ask1 Acsupporting

confidence: 92%

Protein Kinase D Specifically Mediates Apoptosis Signal-regulating Kinase 1-JNK Signaling Induced by H2O2 but Not Tumor Necrosis Factor

Zhang

Zheng

Störz

et al. 2005

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Section: A Critical Role Of Pkd In Mediating H 2 O 2 -Induced Ask1 Acsupporting

confidence: 92%

Protein Kinase D Specifically Mediates Apoptosis Signal-regulating Kinase 1-JNK Signaling Induced by H2O2 but Not Tumor Necrosis Factor

Zhang

Zheng

Störz

et al. 2005

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

“…Transfection of HUVEC was performed by DEAE-Dextran method and BAECs were transfected by Lipofactamine 2000 (Gibco) as described. 27,31,32 Luciferase activity followed by renilla activity was measured twice in duplicate using a Berthold luminometer. All data were normalized as relative luciferase light units/ renilla unit.…”

Section: Methodsmentioning

confidence: 99%

“…In vitro kinase assay using GST-c-Jun and GST-SENP1 was performed as described previously. 27,31,32 Immunoprecipitation and immunoblotting. HUVECs or BAECs after various treatments were washed twice with cold PBS and lysed in 1.5 ml of cold lysis buffer (50 mM Tris-HCl, pH 7.6, 150 mM NaCl, 0.1% Triton X-100, 0.75% Brij 96, 1 mM sodium orthovanadate, 1 mM sodium fluoride, 1 mM sodium pyrophosphate, 10 mg/ml aprotinin, 10 mg/ml leupeptin, 2 mM PMSF and 1 mM EDTA) for 20 min on ice.…”

Section: Methodsmentioning

confidence: 99%

“…23,24 In vitro data suggest that activation of ASK1 triggers various biological responses, such as apoptosis, inflammation, differentiation, and survival in different cell types. [25][26][27][28] Studies from ASK1-deficient mice indicate that ASK1 is critical for TNF-and ROS-induced apoptosis signaling. 29 The mechanism by which stress stimuli activate ASK1 is not fully understood.…”

mentioning

confidence: 99%

See 1 more Smart Citation

SENP1 mediates TNF-induced desumoylation and cytoplasmic translocation of HIPK1 to enhance ASK1-dependent apoptosis

Luo

et al. 2008

Cell Death Differ

View full text Add to dashboard Cite

We have previously shown that tumor necrosis factor (TNF)-induced desumoylation and subsequent cytoplasmic translocation of HIPK1 are critical for ASK1-JNK activation. However, the mechanism by which TNF induces desumoylation of HIPK1 is unclear. Here, we show that SENP1, a SUMO-specific protease, specifically deconjugates SUMO from HIPK1 in vitro and in vivo. In resting endothelial cells (ECs), SENP1 is localized in the cytoplasm where it is complexed with an antioxidant protein thioredoxin. TNF induces the release of SENP1 from thioredoxin as well as nuclear translocation of SENP1. TNF-induced SENP1 nuclear translocation is specifically blocked by antioxidants such as N-acetyl-cysteine, suggesting that TNF-induced translocation of SENP1 is ROS dependent. TNF-induced nuclear import of SENP1 kinetically correlates with HIPK1 desumoylation and cytoplasmic translocation. Furthermore, the wild-type form of SENP1 enhances, whereas the catalyticinactive mutant form or siRNA of SENP1 blocks, TNF-induced desumoylation and cytoplasmic translocation of HIPK1 as well as TNF-induced ASK1-JNK activation. More importantly, these critical functions of SENP1 in TNF signaling were further confirmed in mouse embryonic fibroblast cells derived from SENP1-knockout mice. We conclude that SENP1 mediates TNF-induced desumoylation and translocation of HIPK1, leading to an enhanced ASK1-dependent apoptosis. The small ubiquitin-like modifier (SUMO) can be covalently attached to a large number of proteins through the formation of isopeptide bonds with specific lysine residues of target proteins. 1,2 A large number of sumoylated proteins, including RanGAP1, PML, homeodomain-interacting protein kinases (HIPKs), IkB, p53, c-Jun, Sp3, Elk-1, p300 histone acetyltransferase, histone deacetylase (HDAC), and many nuclear receptors, have been identified. 1-3 Sumoylation is a dynamic process that is mediated by activating, conjugating, and ligating enzymes and that is readily reversed by a family of SUMO-specific proteases. 4 Several members of SUMOspecific proteases have been reported in the mammalian system. 5-10 SENP1 is a protease that appears to deconjugate a large number of sumoylated proteins. 5 Different members of these SUMO-specific proteases appear to localize in different cellular compartments where they regulate protein function by modifying the protein stability, cellular localization, and protein-protein interactions. 5,6,[8][9][10][11][12] However, it is not known how these SUMO-specific proteases are regulated.HIPK1 is one of three closely related serine/threonine protein kinases that are primarily localized in the nucleus where it is sumoylated. 13,14 The HIPKs were originally identified as nuclear protein kinases that function as co-repressors for various homeodomain-containing transcription factors. 15 Recently, HIPKs have been shown to interact with other proteins involved in apoptosis and signal transduction in a cellular localization-dependent manner. In nucleus, HIPK2 phosphorylates p53 on Ser 46, resulting in the activatio...

show abstract

“…JNK Kinase Assay-JNK assays were performed as described previously using glutathione S-transferase-c-Jun-(1-80) fusion protein as a substrate (32). Briefly, a total of 400 g of cell lysates were immunoprecipitated with 5 g of antibody against JNK1 (Santa Cruz).…”

Section: Methodsmentioning

confidence: 99%

Etk/Bmx Transactivates Vascular Endothelial Growth Factor 2 and Recruits Phosphatidylinositol 3-Kinase to Mediate the Tumor Necrosis Factor-induced Angiogenic Pathway

Zhang

Ekman

et al. 2003

Journal of Biological Chemistry

Self Cite

140

129

View full text Add to dashboard Cite

Laminar flow inhibits TNF-induced ASK1 activation by preventing dissociation of ASK1 from its inhibitor 14-3-3

Cited by 107 publications

References 37 publications

Protein Kinase D Specifically Mediates Apoptosis Signal-regulating Kinase 1-JNK Signaling Induced by H2O2 but Not Tumor Necrosis Factor

Protein Kinase D Specifically Mediates Apoptosis Signal-regulating Kinase 1-JNK Signaling Induced by H2O2 but Not Tumor Necrosis Factor

SENP1 mediates TNF-induced desumoylation and cytoplasmic translocation of HIPK1 to enhance ASK1-dependent apoptosis

Etk/Bmx Transactivates Vascular Endothelial Growth Factor 2 and Recruits Phosphatidylinositol 3-Kinase to Mediate the Tumor Necrosis Factor-induced Angiogenic Pathway

Contact Info

Product

Resources

About