22 research outputs found
Quantitative Phosphoproteomic Analysis of Early Alterations in Protein Phosphorylation by 2,3,7,8-Tetrachlorodibenzo‑<i>p</i>‑dioxin
A comprehensive quantitative analysis of changes in protein
phosphorylation
preceding or accompanying transcriptional activation by 2,3,7,8-tetrachlorodibenzo-<i>p</i>-dioxin (TCDD) in 5L rat hepatoma cells was performed using
the SILAC approach. Following exposure of the cells to DMSO or 1 nM
TCDD for 0.5 to 2 h, 5648 phosphorylated peptides corresponding to
2156 phosphoproteins were identified. Eight peptides exhibited a statistically
significantly altered phosphorylation because of TCDD exposure and
22 showed a regulation factor of ≥1.5 in one of the experiments
per time point. The vast majority of the TCCD-induced phosphorylation
changes had not been reported before. The transcription factor ARNT,
the obligate partner for gene activation by the TCDD-bound Ah receptor,
exhibited an up-regulation of its Ser77 phosphorylation, a modification
known to control the differential binding of ARNT homodimers and heterodimers
to different enhancers suggesting that this phosphorylation represents
a novel mechanism contributing to the alteration of gene expression
by TCDD. Other proteins with altered phosphorylation included, among
others, various transcriptional coregulators previously unknown to
participate in TCDD-induced gene activation, regulators of small GTPases
of the Ras superfamily, UBX domain-containing proteins and the oncogenic
protein LYRIC. The results open up new directions for research on
the molecular mechanisms of dioxin action and toxicity
Quantitative Phosphoproteomic Analysis of Early Alterations in Protein Phosphorylation by 2,3,7,8-Tetrachlorodibenzo‑<i>p</i>‑dioxin
A comprehensive quantitative analysis of changes in protein
phosphorylation
preceding or accompanying transcriptional activation by 2,3,7,8-tetrachlorodibenzo-<i>p</i>-dioxin (TCDD) in 5L rat hepatoma cells was performed using
the SILAC approach. Following exposure of the cells to DMSO or 1 nM
TCDD for 0.5 to 2 h, 5648 phosphorylated peptides corresponding to
2156 phosphoproteins were identified. Eight peptides exhibited a statistically
significantly altered phosphorylation because of TCDD exposure and
22 showed a regulation factor of ≥1.5 in one of the experiments
per time point. The vast majority of the TCCD-induced phosphorylation
changes had not been reported before. The transcription factor ARNT,
the obligate partner for gene activation by the TCDD-bound Ah receptor,
exhibited an up-regulation of its Ser77 phosphorylation, a modification
known to control the differential binding of ARNT homodimers and heterodimers
to different enhancers suggesting that this phosphorylation represents
a novel mechanism contributing to the alteration of gene expression
by TCDD. Other proteins with altered phosphorylation included, among
others, various transcriptional coregulators previously unknown to
participate in TCDD-induced gene activation, regulators of small GTPases
of the Ras superfamily, UBX domain-containing proteins and the oncogenic
protein LYRIC. The results open up new directions for research on
the molecular mechanisms of dioxin action and toxicity
Quantitative Phosphoproteomic Analysis of Early Alterations in Protein Phosphorylation by 2,3,7,8-Tetrachlorodibenzo‑<i>p</i>‑dioxin
A comprehensive quantitative analysis of changes in protein
phosphorylation
preceding or accompanying transcriptional activation by 2,3,7,8-tetrachlorodibenzo-<i>p</i>-dioxin (TCDD) in 5L rat hepatoma cells was performed using
the SILAC approach. Following exposure of the cells to DMSO or 1 nM
TCDD for 0.5 to 2 h, 5648 phosphorylated peptides corresponding to
2156 phosphoproteins were identified. Eight peptides exhibited a statistically
significantly altered phosphorylation because of TCDD exposure and
22 showed a regulation factor of ≥1.5 in one of the experiments
per time point. The vast majority of the TCCD-induced phosphorylation
changes had not been reported before. The transcription factor ARNT,
the obligate partner for gene activation by the TCDD-bound Ah receptor,
exhibited an up-regulation of its Ser77 phosphorylation, a modification
known to control the differential binding of ARNT homodimers and heterodimers
to different enhancers suggesting that this phosphorylation represents
a novel mechanism contributing to the alteration of gene expression
by TCDD. Other proteins with altered phosphorylation included, among
others, various transcriptional coregulators previously unknown to
participate in TCDD-induced gene activation, regulators of small GTPases
of the Ras superfamily, UBX domain-containing proteins and the oncogenic
protein LYRIC. The results open up new directions for research on
the molecular mechanisms of dioxin action and toxicity
Quantitative Phosphoproteomic Analysis of Early Alterations in Protein Phosphorylation by 2,3,7,8-Tetrachlorodibenzo‑<i>p</i>‑dioxin
A comprehensive quantitative analysis of changes in protein
phosphorylation
preceding or accompanying transcriptional activation by 2,3,7,8-tetrachlorodibenzo-<i>p</i>-dioxin (TCDD) in 5L rat hepatoma cells was performed using
the SILAC approach. Following exposure of the cells to DMSO or 1 nM
TCDD for 0.5 to 2 h, 5648 phosphorylated peptides corresponding to
2156 phosphoproteins were identified. Eight peptides exhibited a statistically
significantly altered phosphorylation because of TCDD exposure and
22 showed a regulation factor of ≥1.5 in one of the experiments
per time point. The vast majority of the TCCD-induced phosphorylation
changes had not been reported before. The transcription factor ARNT,
the obligate partner for gene activation by the TCDD-bound Ah receptor,
exhibited an up-regulation of its Ser77 phosphorylation, a modification
known to control the differential binding of ARNT homodimers and heterodimers
to different enhancers suggesting that this phosphorylation represents
a novel mechanism contributing to the alteration of gene expression
by TCDD. Other proteins with altered phosphorylation included, among
others, various transcriptional coregulators previously unknown to
participate in TCDD-induced gene activation, regulators of small GTPases
of the Ras superfamily, UBX domain-containing proteins and the oncogenic
protein LYRIC. The results open up new directions for research on
the molecular mechanisms of dioxin action and toxicity
Quantitative Phosphoproteomic Analysis of Early Alterations in Protein Phosphorylation by 2,3,7,8-Tetrachlorodibenzo‑<i>p</i>‑dioxin
A comprehensive quantitative analysis of changes in protein
phosphorylation
preceding or accompanying transcriptional activation by 2,3,7,8-tetrachlorodibenzo-<i>p</i>-dioxin (TCDD) in 5L rat hepatoma cells was performed using
the SILAC approach. Following exposure of the cells to DMSO or 1 nM
TCDD for 0.5 to 2 h, 5648 phosphorylated peptides corresponding to
2156 phosphoproteins were identified. Eight peptides exhibited a statistically
significantly altered phosphorylation because of TCDD exposure and
22 showed a regulation factor of ≥1.5 in one of the experiments
per time point. The vast majority of the TCCD-induced phosphorylation
changes had not been reported before. The transcription factor ARNT,
the obligate partner for gene activation by the TCDD-bound Ah receptor,
exhibited an up-regulation of its Ser77 phosphorylation, a modification
known to control the differential binding of ARNT homodimers and heterodimers
to different enhancers suggesting that this phosphorylation represents
a novel mechanism contributing to the alteration of gene expression
by TCDD. Other proteins with altered phosphorylation included, among
others, various transcriptional coregulators previously unknown to
participate in TCDD-induced gene activation, regulators of small GTPases
of the Ras superfamily, UBX domain-containing proteins and the oncogenic
protein LYRIC. The results open up new directions for research on
the molecular mechanisms of dioxin action and toxicity
Quantitative Phosphoproteomic Analysis of Early Alterations in Protein Phosphorylation by 2,3,7,8-Tetrachlorodibenzo‑<i>p</i>‑dioxin
A comprehensive quantitative analysis of changes in protein
phosphorylation
preceding or accompanying transcriptional activation by 2,3,7,8-tetrachlorodibenzo-<i>p</i>-dioxin (TCDD) in 5L rat hepatoma cells was performed using
the SILAC approach. Following exposure of the cells to DMSO or 1 nM
TCDD for 0.5 to 2 h, 5648 phosphorylated peptides corresponding to
2156 phosphoproteins were identified. Eight peptides exhibited a statistically
significantly altered phosphorylation because of TCDD exposure and
22 showed a regulation factor of ≥1.5 in one of the experiments
per time point. The vast majority of the TCCD-induced phosphorylation
changes had not been reported before. The transcription factor ARNT,
the obligate partner for gene activation by the TCDD-bound Ah receptor,
exhibited an up-regulation of its Ser77 phosphorylation, a modification
known to control the differential binding of ARNT homodimers and heterodimers
to different enhancers suggesting that this phosphorylation represents
a novel mechanism contributing to the alteration of gene expression
by TCDD. Other proteins with altered phosphorylation included, among
others, various transcriptional coregulators previously unknown to
participate in TCDD-induced gene activation, regulators of small GTPases
of the Ras superfamily, UBX domain-containing proteins and the oncogenic
protein LYRIC. The results open up new directions for research on
the molecular mechanisms of dioxin action and toxicity
Quantitative Phosphoproteomic Analysis of Early Alterations in Protein Phosphorylation by 2,3,7,8-Tetrachlorodibenzo‑<i>p</i>‑dioxin
A comprehensive quantitative analysis of changes in protein
phosphorylation
preceding or accompanying transcriptional activation by 2,3,7,8-tetrachlorodibenzo-<i>p</i>-dioxin (TCDD) in 5L rat hepatoma cells was performed using
the SILAC approach. Following exposure of the cells to DMSO or 1 nM
TCDD for 0.5 to 2 h, 5648 phosphorylated peptides corresponding to
2156 phosphoproteins were identified. Eight peptides exhibited a statistically
significantly altered phosphorylation because of TCDD exposure and
22 showed a regulation factor of ≥1.5 in one of the experiments
per time point. The vast majority of the TCCD-induced phosphorylation
changes had not been reported before. The transcription factor ARNT,
the obligate partner for gene activation by the TCDD-bound Ah receptor,
exhibited an up-regulation of its Ser77 phosphorylation, a modification
known to control the differential binding of ARNT homodimers and heterodimers
to different enhancers suggesting that this phosphorylation represents
a novel mechanism contributing to the alteration of gene expression
by TCDD. Other proteins with altered phosphorylation included, among
others, various transcriptional coregulators previously unknown to
participate in TCDD-induced gene activation, regulators of small GTPases
of the Ras superfamily, UBX domain-containing proteins and the oncogenic
protein LYRIC. The results open up new directions for research on
the molecular mechanisms of dioxin action and toxicity
Quantitative Phosphoproteomic Analysis of Early Alterations in Protein Phosphorylation by 2,3,7,8-Tetrachlorodibenzo‑<i>p</i>‑dioxin
A comprehensive quantitative analysis of changes in protein
phosphorylation
preceding or accompanying transcriptional activation by 2,3,7,8-tetrachlorodibenzo-<i>p</i>-dioxin (TCDD) in 5L rat hepatoma cells was performed using
the SILAC approach. Following exposure of the cells to DMSO or 1 nM
TCDD for 0.5 to 2 h, 5648 phosphorylated peptides corresponding to
2156 phosphoproteins were identified. Eight peptides exhibited a statistically
significantly altered phosphorylation because of TCDD exposure and
22 showed a regulation factor of ≥1.5 in one of the experiments
per time point. The vast majority of the TCCD-induced phosphorylation
changes had not been reported before. The transcription factor ARNT,
the obligate partner for gene activation by the TCDD-bound Ah receptor,
exhibited an up-regulation of its Ser77 phosphorylation, a modification
known to control the differential binding of ARNT homodimers and heterodimers
to different enhancers suggesting that this phosphorylation represents
a novel mechanism contributing to the alteration of gene expression
by TCDD. Other proteins with altered phosphorylation included, among
others, various transcriptional coregulators previously unknown to
participate in TCDD-induced gene activation, regulators of small GTPases
of the Ras superfamily, UBX domain-containing proteins and the oncogenic
protein LYRIC. The results open up new directions for research on
the molecular mechanisms of dioxin action and toxicity
Quantitative Phosphoproteomic Analysis of Early Alterations in Protein Phosphorylation by 2,3,7,8-Tetrachlorodibenzo‑<i>p</i>‑dioxin
A comprehensive quantitative analysis of changes in protein
phosphorylation
preceding or accompanying transcriptional activation by 2,3,7,8-tetrachlorodibenzo-<i>p</i>-dioxin (TCDD) in 5L rat hepatoma cells was performed using
the SILAC approach. Following exposure of the cells to DMSO or 1 nM
TCDD for 0.5 to 2 h, 5648 phosphorylated peptides corresponding to
2156 phosphoproteins were identified. Eight peptides exhibited a statistically
significantly altered phosphorylation because of TCDD exposure and
22 showed a regulation factor of ≥1.5 in one of the experiments
per time point. The vast majority of the TCCD-induced phosphorylation
changes had not been reported before. The transcription factor ARNT,
the obligate partner for gene activation by the TCDD-bound Ah receptor,
exhibited an up-regulation of its Ser77 phosphorylation, a modification
known to control the differential binding of ARNT homodimers and heterodimers
to different enhancers suggesting that this phosphorylation represents
a novel mechanism contributing to the alteration of gene expression
by TCDD. Other proteins with altered phosphorylation included, among
others, various transcriptional coregulators previously unknown to
participate in TCDD-induced gene activation, regulators of small GTPases
of the Ras superfamily, UBX domain-containing proteins and the oncogenic
protein LYRIC. The results open up new directions for research on
the molecular mechanisms of dioxin action and toxicity
Quantitative Phosphoproteomic Analysis of Early Alterations in Protein Phosphorylation by 2,3,7,8-Tetrachlorodibenzo‑<i>p</i>‑dioxin
A comprehensive quantitative analysis of changes in protein
phosphorylation
preceding or accompanying transcriptional activation by 2,3,7,8-tetrachlorodibenzo-<i>p</i>-dioxin (TCDD) in 5L rat hepatoma cells was performed using
the SILAC approach. Following exposure of the cells to DMSO or 1 nM
TCDD for 0.5 to 2 h, 5648 phosphorylated peptides corresponding to
2156 phosphoproteins were identified. Eight peptides exhibited a statistically
significantly altered phosphorylation because of TCDD exposure and
22 showed a regulation factor of ≥1.5 in one of the experiments
per time point. The vast majority of the TCCD-induced phosphorylation
changes had not been reported before. The transcription factor ARNT,
the obligate partner for gene activation by the TCDD-bound Ah receptor,
exhibited an up-regulation of its Ser77 phosphorylation, a modification
known to control the differential binding of ARNT homodimers and heterodimers
to different enhancers suggesting that this phosphorylation represents
a novel mechanism contributing to the alteration of gene expression
by TCDD. Other proteins with altered phosphorylation included, among
others, various transcriptional coregulators previously unknown to
participate in TCDD-induced gene activation, regulators of small GTPases
of the Ras superfamily, UBX domain-containing proteins and the oncogenic
protein LYRIC. The results open up new directions for research on
the molecular mechanisms of dioxin action and toxicity