Phosphorylated fragments of the epidermal growth factor receptor: Sequence specificity for binding to phospholipase Cγ1 SH2 domains, and for kinase and phosphatase activity

Peptides ◽  
1994 ◽  
pp. 948-950
Author(s):  
D. Maclean ◽  
A. M. Sefler ◽  
D. J. McNamara ◽  
Z.-Y. Zhang ◽  
G. Zhu ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Phosphatase Activity ◽  
Growth Factor Receptor ◽  
Sequence Specificity ◽  
Sh2 Domains ◽  
Phospholipase Cγ1 ◽  
Epidermal Growth

scholarly journals Conversion of a phosphoseryl/threonyl phosphatase into a phosphotyrosyl phosphatase

1988 ◽  
Vol 256 (3) ◽  
pp. 1029-1034 ◽  
Author(s):  
J Goris ◽  
C J Pallen ◽  
P J Parker ◽  
J Hermann ◽  
M D Waterfield ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Phosphatase Activity ◽  
Growth Factor Receptor ◽  
Xenopus Laevis Oocytes ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Epidermal Growth ◽  
Autophosphorylation Site

By use of the autophosphorylated epidermal-growth-factor receptor and the synthetic peptide RRLIE-DAEY(P)AARG, representing an autophosphorylation site of the transforming protein of Rous-sarcoma virus, it is demonstrated that the phosphotyrosyl phosphatase activity of the polycation-stimulated phosphatases is substantially increased by an enzyme-directed effect of ATP or PPi. Concomitant with this increase in phosphotyrosyl phosphatase activity, the phosphorylase phosphatase activity is decreased, thus dramatically changing the substrate specificity of these enzymes. The dephosphorylation of four different phosphotyrosyl sites of the epidermal-growth-factor receptor is neither consecutive nor at random, but a preferred dephosphorylation of the P1 site over the P3 greater than P2 greater than P4 sites is observed. This phosphatase activity represents a substantial fraction of the total phosphotyrosyl phosphatase activity in the post-mitochondrial supernatant of Xenopus laevis oocytes.

scholarly journals Association of Tyrosine Phosphatase Epsilon with Microtubules Inhibits Phosphatase Activity and Is Regulated by the Epidermal Growth Factor Receptor

2007 ◽  
Vol 27 (20) ◽  
pp. 7102-7112 ◽  
Author(s):  
Tal Sines ◽  
Shira Granot-Attas ◽  
Sabrina Weisman-Welcher ◽  
Ari Elson
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Phosphatase Activity ◽  
Specific Activity ◽  
Tyrosine Phosphatase ◽  
Growth Factor Receptor ◽  
Epidermal Growth ◽  
In Cells

ABSTRACT Protein tyrosine phosphatases (PTPs) are key mediators that link physiological cues with reversible changes in protein structure and function; nevertheless, significant details concerning their regulation in vivo remain unknown. We demonstrate that PTPε associates with microtubules in vivo and is inhibited by them in a noncompetitive manner. Microtubule-associated proteins, which interact strongly with microtubules in vivo, significantly increase binding of PTPε to tubulin in vitro and further reduce phosphatase activity. Conversely, disruption of microtubule structures in cells reduces their association with PTPε, alters the subcellular localization of the phosphatase, and increases its specific activity. Activation of the epidermal growth factor receptor (EGFR) increases the PTPε-microtubule association in a manner dependent upon EGFR-induced phosphorylation of PTPε at Y638 and upon microtubule integrity. These events are transient and occur with rapid kinetics similar to EGFR autophosphorylation, suggesting that activation of the EGFR transiently down-regulates PTPε activity near the receptor by promoting the PTPε-microtubule association. Tubulin also inhibits the tyrosine phosphatase PTP1B but not receptor-type PTPμ or the unrelated alkaline phosphatase. The data suggest that reversible association with microtubules is a novel, physiologically regulated mechanism for regulation of tyrosine phosphatase activity in cells.

scholarly journals Selective regulation of clathrin-mediated epidermal growth factor receptor signaling and endocytosis by phospholipase C and calcium

2017 ◽  
Vol 28 (21) ◽  
pp. 2802-2818 ◽  
Author(s):  
Ralph Christian Delos Santos ◽  
Stephen Bautista ◽  
Stefanie Lucarelli ◽  
Leslie N. Bone ◽  
Roya M. Dayam ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Surface Protein ◽  
Egfr Signaling ◽  
Coated Pits ◽  
Cellular Processes ◽  
Phospholipase Cγ1 ◽  
Epidermal Growth

Clathrin-mediated endocytosis is a major regulator of cell-surface protein internalization. Clathrin and other proteins assemble into small invaginating structures at the plasma membrane termed clathrin-coated pits (CCPs) that mediate vesicle formation. In addition, epidermal growth factor receptor (EGFR) signaling is regulated by its accumulation within CCPs. Given the diversity of proteins regulated by clathrin-mediated endocytosis, how this process may distinctly regulate specific receptors is a key question. We examined the selective regulation of clathrin-dependent EGFR signaling and endocytosis. We find that perturbations of phospholipase Cγ1 (PLCγ1), Ca2+, or protein kinase C (PKC) impair clathrin-mediated endocytosis of EGFR, the formation of CCPs harboring EGFR, and EGFR signaling. Each of these manipulations was without effect on the clathrin-mediated endocytosis of transferrin receptor (TfR). EGFR and TfR were recruited to largely distinct clathrin structures. In addition to control of initiation and assembly of CCPs, EGF stimulation also elicited a Ca2+- and PKC-dependent reduction in synaptojanin1 recruitment to clathrin structures, indicating broad control of CCP assembly by Ca2+ signals. Hence EGFR elicits PLCγ1-calcium signals to facilitate formation of a subset of CCPs, thus modulating its own signaling and endocytosis. This provides evidence for the versatility of CCPs to control diverse cellular processes.

scholarly journals Both SH2 Domains Are Involved in Interaction of SHP-1 with the Epidermal Growth Factor Receptor but Cannot Confer Receptor-directed Activity to SHP-1/SHP-2 Chimera

1997 ◽  
Vol 272 (9) ◽  
pp. 5966-5973 ◽  
Author(s):  
Tencho Tenev ◽  
Heike Keilhack ◽  
Sinisa Tomic ◽  
Boris Stoyanov ◽  
Matthias Stein-Gerlach ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Sh2 Domains ◽  
Epidermal Growth
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