An SH3-SH2-SH3 protein is required for p21(Ras 1) activation and binds to sevenless and Sos proteins in vitro
Article Abstract:
A study examines the processes involved when the Drosophila melanogaster's sevenless gene encodes the signal of the receptor protein-tyrosine kinase. One of the main results is that a gene named E(sev)2B, which is required for proper signaling by sevenless, encodes a protein of the structure SH3-SH2-SH3 and is required for and only for the activation of p21(Ras 1). Moreover, the E(sev)2B protein can bind in vitro to sevenless and to Son of sevenless, a putative quanine nucleotide exchange factor for p21(Ras 1). Thus, this protein may help Sos activate p21(Ras 1) by applying a signaling complex.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
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CNK, a RAF-binding multidomain protein required for RAS signaling
Article Abstract:
The connector enhancer of the kinase suppressor (CNK) of the reticular activating system (RAS) appeared to function in the RAS pathway upstream or in parallel to the RAF kinase in transducing signals elicited by receptor tyrosine kinases. It was shown that overexpressed CNK localizes to regions of cell-cell contact and relates physically with Drosophila RAF. These findings suggested that CNK is a novel component of the RAS/mitogen-activated protein kinase pathway that may function to regulate activity or the subcellular localization of RAF following RAS activation.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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TAFIIS mediate activation of transcription in the Drosophila embryo
Article Abstract:
The role of transcription-activating factors (TAF) such as TAFII60 and TAFII110 in the embryonic development of Drosophila was analyzed by utilizing genetic test systems. TAFII60 and TAFII110 mutants exhibited impaired TAF functions due to the inability of the trancription factors to participate in protein-protein interactions. Furthermore, the TAF mutants altered bicoid-dependent activation of transcription in vitro due to impaired interactions with TAFII250.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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