1,721,030 research outputs found
DNA encoding human and murine EPS15, a substrate for the epidermal growth factor receptor
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Identification and biochemical characterization of novel putative substrates for the epidermal growth factor receptor kinase.
No full texterbB-2 autophosphorylation is required for mitogenic action and high-affinity substrate coupling.
No full textThe carboxy-terminal domains of erbB-2 and epidermal growth factor receptor exert different regulatory effects on intrinsic receptor tyrosine kinase function and transforming activity.
No full textEps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signals.
No full textAll ErbB receptors other than epidermal growth factor receptor are endocytosis impaired
Full text linkFour transmembrane tyrosine kinases constitute the
ErbB receptor family: the epidermal growth factor
(EGF) receptor, ErbB-2, ErbB-3, and ErbB-4. We have
measured the endocytic capacities of all four members
of the EGF receptor family, including ErbB-3 and
ErbB-4, which have not been described previously. EGFresponsive
chimeric receptors containing the EGF receptor
extracellular domain and different ErbB cytoplasmic
domains (EGFR/ErbB) have been employed. The
capacity of these growth factor-receptor complexes to
mediate 125I-EGF internalization, receptor down-regulation,
receptor degradation, and receptor co-immunoprecipitation
with AP-2 was assayed. In contrast to the EGF
receptor, all EGFR/ErbB receptors show impaired ligand-
induced rapid internalization, down-regulation,
degradation, and AP-2 association. Also, we have analyzed
the heregulin-responsive wild-type ErbB-4 receptor,
which does not mediate the rapid internalization of
125I-heregulin, demonstrates no heregulin-regulated receptor
degradation, and fails to form association complexes
with AP-2. Despite the substantial differences in
ligand-induced receptor trafficking between the EGF
and ErbB-4 receptors, EGF and heregulin have equivalent
capacities to stimulate DNA synthesis in quiescent
cells. These results show that the ligand-dependent
down-regulation mechanism of the EGF receptor, surprisingly,
is not a property of any other known ErbB
receptor family member. Since endocytosis is thought to
be an attenuation mechanism for growth factor-receptor
complexes, these data imply that substantial differences
in attenuation mechanisms exist within one family
of structurally related receptors
The ezrin-like family of tyrosine kinase substrates: receptor-specific pattern of tyrosine phosphorylation and relationship to malignant transformation.
No full textDirect binding of eps8 to the juxtamembrane domain of EGFR is phosphotyrosine- and SH2-independent.
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