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Physiol. Genomics 8: 41-50, 2002. First published November 20, 2001; doi:10.1152/physiolgenomics.00085.2001
1094-8341/02 $5.00
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Received 25 September 2001; accepted in final form 17 November 2001.
Physiological Genomics 8:41-50 (2002)
1094-8341/02 $5.00 © 2002 American Physiological Society

Cloning, tissue distribution, and functional expression of the human G protein ß4-subunit

VICTOR RUIZ-VELASCO1, STEPHEN R. IKEDA1,2 and HENRY L. PUHL2

1 Laboratory of Molecular Physiology
2 cDNA Resource Center, Guthrie Research Institute, Sayre, Pennsylvania 18840

Heterotrimeric G proteins (G{alpha}ß{gamma}) play an essential role in coupling membrane receptors to effector proteins such as ion channels and enzymes. Among the five mammalian Gß-subunits cloned, the human G protein ß4 has not been described. The purpose of the present study was to functionally characterize the newly identified human Gß4 subunit. The Gß4 open reading frame (ORF) was amplified utilizing PCR from brain cDNA. Amplification primers were generated following 5' rapid amplification of cDNA ends (5'-RACE) from an expressed sequence tag (EST) containing the predicted 3' end of the protein. Multiple tissue cDNA panel analysis showed that Gß4 mRNA was strongly expressed in lung and placenta, whereas it is weakly expressed in brain and heart. Heterologous overexpression of Gß4{gamma}2 or Gß4{gamma}4 in rat sympathetic neurons resulted in tonic modulation of N-type voltage-gated Ca2+ and G protein-gated inwardly rectifying K+ currents. Furthermore, coexpression of Gß4{gamma}2 and G{alpha}oA resulted in heterotrimer formation. These results show that the newly cloned Gß4 subunit shares several properties with other human Gß family members.

G protein ß4; signal transduction; ion channel modulation




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