Abstract
The aim of this study was the characterization of the human Gbeta4 subunit of heterotrimeric G proteins. Human Gbeta4 is widely expressed. Its gene is located on chromosome 3 with a genomic structure indistinguishable from that of the genes of Gbeta1 to Gbeta3, but entirely different from Gbeta5. In vitro translation co-precipitation analyses revealed that Gbeta4 can form stable dimers with Ggamma1, Ggamma2, Ggamma3, Ggamma4, Ggamma5, Ggamma7, Ggamma10, Ggamma11, Ggamma12, and Ggamma13, dimers which were also able to stimulate phospholipase beta2.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Chromosomes, Human, Pair 3
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Cloning, Molecular
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DNA, Complementary / metabolism
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Dimerization
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Enzyme Activation
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Exons
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Heterotrimeric GTP-Binding Proteins / chemistry*
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Heterotrimeric GTP-Binding Proteins / genetics*
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Heterotrimeric GTP-Binding Proteins / metabolism*
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Humans
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Models, Genetic
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Molecular Sequence Data
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Precipitin Tests
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Protein Biosynthesis
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Protein Structure, Tertiary
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RNA, Messenger / metabolism
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Reverse Transcriptase Polymerase Chain Reaction
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Signal Transduction
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Tissue Distribution
Substances
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DNA, Complementary
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RNA, Messenger
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Heterotrimeric GTP-Binding Proteins