Abstract
Transcription factor p91 contains a SH2 domain and is activated by tyrosine phosphorylation. Here we demonstrate that epidermal growth factor (EGF) induces rapid tyrosine phosphorylation and nuclear translocation of p91. Through its SH2 domain, p91 directly interacts with the EGF receptor in a ligand-dependent manner. p91 is a necessary component of an EGF-induced DNA-binding factor that recognizes a previously identified regulatory element, SIE (c-sis-inducible element), in the c-fos gene promoter. Activated p91 stimulates SIE-dependent transcription in vitro. Cotransfection of an SIE-containing reporter with a p91 expression vector shows that p91 is a positive transcriptional regulator of the c-fos gene promoter. These studies suggest that EGF uses a direct signaling pathway to control nuclear transcriptional events.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1135-1145 |
| Number of pages | 11 |
| Journal | Cell |
| Volume | 74 |
| Issue number | 6 |
| DOIs | |
| State | Published - Sep 24 1993 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Cell Biology
- Molecular Biology
Cite this
Transcription factor p91 interacts with the epidermal growth factor receptor and mediates activation of the c-fos gene promoter. / Fu, Xin Yuan; Zhang, Jiao Jiao.
In: Cell, Vol. 74, No. 6, 24.09.1993, p. 1135-1145.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Transcription factor p91 interacts with the epidermal growth factor receptor and mediates activation of the c-fos gene promoter
AU - Fu, Xin Yuan
AU - Zhang, Jiao Jiao
PY - 1993/9/24
Y1 - 1993/9/24
N2 - Transcription factor p91 contains a SH2 domain and is activated by tyrosine phosphorylation. Here we demonstrate that epidermal growth factor (EGF) induces rapid tyrosine phosphorylation and nuclear translocation of p91. Through its SH2 domain, p91 directly interacts with the EGF receptor in a ligand-dependent manner. p91 is a necessary component of an EGF-induced DNA-binding factor that recognizes a previously identified regulatory element, SIE (c-sis-inducible element), in the c-fos gene promoter. Activated p91 stimulates SIE-dependent transcription in vitro. Cotransfection of an SIE-containing reporter with a p91 expression vector shows that p91 is a positive transcriptional regulator of the c-fos gene promoter. These studies suggest that EGF uses a direct signaling pathway to control nuclear transcriptional events.
AB - Transcription factor p91 contains a SH2 domain and is activated by tyrosine phosphorylation. Here we demonstrate that epidermal growth factor (EGF) induces rapid tyrosine phosphorylation and nuclear translocation of p91. Through its SH2 domain, p91 directly interacts with the EGF receptor in a ligand-dependent manner. p91 is a necessary component of an EGF-induced DNA-binding factor that recognizes a previously identified regulatory element, SIE (c-sis-inducible element), in the c-fos gene promoter. Activated p91 stimulates SIE-dependent transcription in vitro. Cotransfection of an SIE-containing reporter with a p91 expression vector shows that p91 is a positive transcriptional regulator of the c-fos gene promoter. These studies suggest that EGF uses a direct signaling pathway to control nuclear transcriptional events.
UR - http://www.scopus.com/inward/record.url?scp=0027372119&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027372119&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(93)90734-8
DO - 10.1016/0092-8674(93)90734-8
M3 - Article
VL - 74
SP - 1135
EP - 1145
JO - Cell
JF - Cell
SN - 0092-8674
IS - 6
ER -