A putative tyrosine phosphorylation site of the cell surface receptor Golden goal is involved in synaptic layer selection in the visual system

Development ◽  
2012 ◽  
Vol 139 (4) ◽  
pp. 760-771 ◽  
Author(s):  
K. Mann ◽  
M. Wang ◽  
S.-H. Luu ◽  
S. Ohler ◽  
S. Hakeda-Suzuki ◽  
...  
Keyword(s):  
Cell Surface ◽  
Visual System ◽  
Tyrosine Phosphorylation ◽  
Phosphorylation Site ◽  
Cell Surface Receptor ◽  
Surface Receptor ◽  
Tyrosine Phosphorylation Site

scholarly journals Association of the tyrosine phosphorylated epidermal growth factor receptor with a 55-kD tyrosine phosphorylated protein at the cell surface and in endosomes.

1992 ◽  
Vol 116 (2) ◽  
pp. 321-330 ◽  
Author(s):  
I Wada ◽  
W H Lai ◽  
B I Posner ◽  
J J Bergeron
Keyword(s):  
Cell Surface ◽  
Tyrosine Phosphorylation ◽  
Plasma Membranes ◽  
Egf Receptor ◽  
Limited Proteolysis ◽  
Specific Radioactivity ◽  
Growth Factor Receptor ◽  
Gel Permeation Chromatography ◽  
Cell Surface Receptor ◽  
Surface Receptor

After the intraportal injection of EGF, the EGF receptor (EGFR) is rapidly internalized into hepatic endosomes where it remains largely receptor bound (Lai et al., 1989. J. Cell Biol. 109:2751-2760). In the present study, we evaluated the phosphotyrosine content of EGFRs at the cell surface and in endosomes in order to assess the consequences of internalization. Quantitative estimates of specific radioactivity of the EGFR in these two compartments revealed that tyrosine phosphorylation of the EGFR was observed at the cell surface within 30 s of ligand administration. However, the EGFR was also highly phosphorylated in endosomes reaching levels of tyrosine phosphorylation significantly higher than those of the cell surface receptor at 5 and 15 min after EGF injection. A 55-kD tyrosine phosphorylated polypeptide (pyp55) was observed in association with the EGFR at the cell surface within 30 s of EGF injection. The protein was also found in association with the EGFR in endosomes as evidenced by coprecipitation studies using a mAb to the EGFR as well as by coelution with the EGR in gel permeation chromatography. Limited proteolysis of isolated endosomes indicated that the tyrosine phosphorylated domains of the EGFR and associated pyp55 were cytosolically oriented while internalized EGF was intraluminal. The identification of pyp55 in association with EGFR in both hepatic plasma membranes and endosomes may be relevant to EGFR function and/or trafficking of the EGFR.

Expression, function, and localization of the REG cell surface receptor

2001 ◽  
Vol 120 (5) ◽  
pp. A18-A19
Author(s):  
B DIECKGRAEFE ◽  
C HOUCHEN ◽  
H ZHANG
Keyword(s):  
Cell Surface ◽  
Cell Surface Receptor ◽  
Surface Receptor

Inhibition of rat ventricular automaticity by adenosine

1985 ◽  
Vol 248 (6) ◽  
pp. H907-H913 ◽  
Author(s):  
L. J. Heller ◽  
R. A. Olsson
Keyword(s):  
Cell Surface ◽  
Cell Surface Receptor ◽  
Chronotropic Effect ◽  
Surface Receptors ◽  
Adenosine Concentration ◽  
Surface Receptor ◽  
Ventricular Automaticity ◽  
Beating Rate ◽  
Chronotropic Effects ◽  
Developed Pressure

This study was designed to characterize adenosine's negative chronotropic effect on ventricular pacemakers. The spontaneous beating rate of isolated, isovolumic rat ventricular preparations perfused with Krebs-Henseleit solution decreased as the adenosine concentration was increased [log M effective concentration 50% (EC50) = -5.22 +/- 0.17]. The lack of effect of propranolol or atropine on this adenosine response eliminates the involvement of endogenous neurotransmitters. Support for the involvement of an external cell surface receptor was provided by findings that theophylline and 8-(4-sulfophenyl)theophylline, an analogue thought to act solely at the cell surface, significantly increased the adenosine log M EC50 to -3.94 +/- 0.22 and -3.61 +/- 0.22, respectively. An increase in spontaneous beating rate induced by theophylline, but not by its analogue, was blocked by the addition of propranolol. The relative chronotropic potency of the adenosine analogues R-PIA, S-PIA, and NECA suggests that the cell surface receptors may be of the Ri type. The negative chronotropic effects of adenosine and its analogues occurred at concentrations that had no effect on the developed pressure of the paced preparation. Electrocardiographic evaluations indicate that at high agonist concentrations, there was an abrupt alteration in electrical properties of the preparation, which could be blocked by theophylline and its analogue.

scholarly journals The cell surface receptor for immunoglobulin E. II. Properties of the purified biologically active receptor.

1979 ◽  
Vol 254 (9) ◽  
pp. 3194-3200
Author(s):  
A. Kulczycki ◽  
B L Hempstead ◽  
S L Hofmann ◽  
E W Wood ◽  
C W Parker
Keyword(s):  
Cell Surface ◽  
Immunoglobulin E ◽  
Biologically Active ◽  
Cell Surface Receptor ◽  
Surface Receptor
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