The Drosophila TGF alpha homolog Spitz acts in photoreceptor recruitment in the developing retina

Development ◽  
1997 ◽  
Vol 124 (2) ◽  
pp. 343-351 ◽  
Author(s):  
M. Tio ◽  
K. Moses

In vertebrates and Drosophila, the Epidermal Growth Factor Receptor (EGFR) signal transduction pathway is important in the regulation of cellular development. EGFR is bound by several activating ligands including Transforming Growth Factor-alpha in vertebrates, and its homolog Spitz in Drosophila. It has been shown that Spitz and EGFR act in the development of the Drosophila central nervous system and compound eye. Here we show that spitz function is required in developing ommatidia for the first cell recruitment step, and that Spitz pro-protein is expressed in the retinal neurons as they begin to differentiate. We propose a ‘two-key’ model for additive signal transduction from EGFR and other receptor tyrosine kinases, via the Ras pathway, in the developing eye.

2005 ◽  
Vol 19 (8) ◽  
pp. 1951-1959 ◽  
Author(s):  
Ellis R. Levin

Abstract Estrogen receptors (ERs) are localized to many sites within the cell, potentially contributing to overall estrogen action. In the nucleus, estrogen mainly modulates gene transcription, and the resulting protein products determine the cell biological actions of the sex steroid. In addition, a small pool of ERs localize to the plasma membrane and signal mainly though coupling, directly or indirectly, to G proteins. In response to steroid, signal transduction modulates both nontranscriptional and transcriptional events and impacts both the rapid and more prolonged actions of estrogen. Cross-talk from membrane-localized ERs to nuclear ERs can be mediated through growth factor receptor tyrosine kinases, such as epidermal growth factor receptor and IGF-I receptor. Growth factor receptors enact signal transduction to kinases such as ERK and phosphatidylinositol 3-kinase that phosphorylate and activate nuclear ERs, and this can also occur in the absence of sex steroid. A complex relationship between the membrane and nuclear effects of estrogen also involves membrane-initiated phosphorylation of coactivators, recruiting these proteins to the nuclear transcriptosome. Finally, large pools of cytoplasmic ERs exist, and some are localized to mitochondria. The integration of sex steroid effects at distinct cellular locations of its receptor leads to important cellular physiological outcomes and are manifest in both reproductive and nonreproductive organs.


Biochemistry ◽  
1992 ◽  
Vol 31 (40) ◽  
pp. 9546-9554 ◽  
Author(s):  
Audrey Richter ◽  
J. Wayne Conlan ◽  
Michael E. Ward ◽  
Stephen G. Chamberlin ◽  
Peter Alexander ◽  
...  

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