siRNA Screen Identifies the Phosphatase Acting on the G Protein-Coupled Thyrotropin-Releasing Hormone Receptor

2012 ◽  
Vol 8 (3) ◽  
pp. 588-598 ◽  
Author(s):  
Austin U. Gehret ◽  
Patricia M. Hinkle
2009 ◽  
Vol 77 (2) ◽  
pp. 288-297 ◽  
Author(s):  
Austin U. Gehret ◽  
Brian W. Jones ◽  
Phuong N. Tran ◽  
Laurie B. Cook ◽  
Emileigh K. Greuber ◽  
...  

1994 ◽  
Vol 303 (1) ◽  
pp. 129-134 ◽  
Author(s):  
N Matus-Leibovitch ◽  
D R Nussenzveig ◽  
M C Gershengorn ◽  
Y Oron

The thyrotropin-releasing-hormone receptor (TRH-R) is a member of a family of the G-protein-coupled receptors that share structural similarities and exert their physiological action via the inositol lipid signal-transduction pathway. The TRH-R when expressed in Xenopus oocytes exhibits marked preference of the response (increased chloride conductance) for the animal hemisphere. Whereas the rat TRH-R functional distribution was strongly asymmetric (animal/vegetal ratio = 9.5), the mouse TRH-R exhibited a significantly lower ratio (3.9). Truncation of the last 59 amino acids of the C-terminal region of the mouse TRH-R did not lead to any changes in the functional hemispheric distribution. Despite the polarization of response, receptor number was similar on both hemispheres. Moreover, the apparent half-life of the functional expression of the TRH-R was approx. 4 h on both hemispheres when the expression was inhibited by a specific antisense oligonucleotide. Inhibition of total protein synthesis with cycloheximide affected hemispheric responses mediated by each of the three TRH-Rs tested in a qualitatively different way. These results suggest that an additional, rapidly degraded, protein modulates the functional hemispheric expression of the TRH-Rs.


2012 ◽  
Vol 227 (6) ◽  
pp. 2492-2501 ◽  
Author(s):  
Sayomi Higa-Nakamine ◽  
Noriko Maeda ◽  
Seikichi Toku ◽  
Tomoko Yamamoto ◽  
Matee Yingyuenyong ◽  
...  

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