Regulation of Stat3 transcriptional activity by the conserved LPMSP motif for OSM and IL-6 signaling

Wei Sun; Marylynn Snyder; David E. Levy; J. Jillian Zhang

doi:10.1016/j.febslet.2006.09.054

Regulation of Stat3 transcriptional activity by the conserved LPMSP motif for OSM and IL-6 signaling

Wei Sun
, Marylynn Snyder
, David E. Levy
, J. Jillian Zhang

Research output: Contribution to journal › Article › peer-review

20 Scopus citations

Abstract

To achieve maximal transcriptional activity in response to gp130 cytokines, Serine-727 (Ser-727) of Stat3 is phosphorylated. Ser-727 resides in the LPMSP motif, the only conserved sequence among the transcription activation domains of several STATs. We show here that in addition to Ser-727, other residues in this LPMSP motif are also required for Stat3 activity in response to cytokine signaling through regulation of Ser-727 phosphorylation and recruitment of the transcription co-activator CBP/p300 to the promoters of Stat3-target genes for transcription activation. Hence, we have demonstrated a critical role for the whole conserved LPMSP motif in JAK-STAT signaling.

Original language	English (US)
Pages (from-to)	5880-5884
Number of pages	5
Journal	FEBS Letters
Volume	580
Issue number	25
DOIs	https://doi.org/10.1016/j.febslet.2006.09.054
State	Published - Oct 30 2006
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Keywords

IL-6
Oncostatin M
Serine phosphorylation
Stat3
Transcription

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10.1016/j.febslet.2006.09.054

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title = "Regulation of Stat3 transcriptional activity by the conserved LPMSP motif for OSM and IL-6 signaling",

abstract = "To achieve maximal transcriptional activity in response to gp130 cytokines, Serine-727 (Ser-727) of Stat3 is phosphorylated. Ser-727 resides in the LPMSP motif, the only conserved sequence among the transcription activation domains of several STATs. We show here that in addition to Ser-727, other residues in this LPMSP motif are also required for Stat3 activity in response to cytokine signaling through regulation of Ser-727 phosphorylation and recruitment of the transcription co-activator CBP/p300 to the promoters of Stat3-target genes for transcription activation. Hence, we have demonstrated a critical role for the whole conserved LPMSP motif in JAK-STAT signaling.",

keywords = "IL-6, Oncostatin M, Serine phosphorylation, Stat3, Transcription",

author = "Wei Sun and Marylynn Snyder and Levy, \{David E.\} and Zhang, \{J. Jillian\}",

year = "2006",

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doi = "10.1016/j.febslet.2006.09.054",

language = "English (US)",

volume = "580",

pages = "5880--5884",

journal = "FEBS Letters",

issn = "0014-5793",

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TY - JOUR

T1 - Regulation of Stat3 transcriptional activity by the conserved LPMSP motif for OSM and IL-6 signaling

AU - Sun, Wei

AU - Snyder, Marylynn

AU - Levy, David E.

AU - Zhang, J. Jillian

PY - 2006/10/30

Y1 - 2006/10/30

N2 - To achieve maximal transcriptional activity in response to gp130 cytokines, Serine-727 (Ser-727) of Stat3 is phosphorylated. Ser-727 resides in the LPMSP motif, the only conserved sequence among the transcription activation domains of several STATs. We show here that in addition to Ser-727, other residues in this LPMSP motif are also required for Stat3 activity in response to cytokine signaling through regulation of Ser-727 phosphorylation and recruitment of the transcription co-activator CBP/p300 to the promoters of Stat3-target genes for transcription activation. Hence, we have demonstrated a critical role for the whole conserved LPMSP motif in JAK-STAT signaling.

AB - To achieve maximal transcriptional activity in response to gp130 cytokines, Serine-727 (Ser-727) of Stat3 is phosphorylated. Ser-727 resides in the LPMSP motif, the only conserved sequence among the transcription activation domains of several STATs. We show here that in addition to Ser-727, other residues in this LPMSP motif are also required for Stat3 activity in response to cytokine signaling through regulation of Ser-727 phosphorylation and recruitment of the transcription co-activator CBP/p300 to the promoters of Stat3-target genes for transcription activation. Hence, we have demonstrated a critical role for the whole conserved LPMSP motif in JAK-STAT signaling.

KW - IL-6

KW - Oncostatin M

KW - Serine phosphorylation

KW - Stat3

KW - Transcription

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U2 - 10.1016/j.febslet.2006.09.054

DO - 10.1016/j.febslet.2006.09.054

M3 - Article

C2 - 17027757

AN - SCOPUS:33750077262

SN - 0014-5793

VL - 580

SP - 5880

EP - 5884

JO - FEBS Letters

JF - FEBS Letters

IS - 25

ER -

Regulation of Stat3 transcriptional activity by the conserved LPMSP motif for OSM and IL-6 signaling

Abstract

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Keywords

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