Interaction Site of GTP Binding Gh (Transglutaminase II) with Phospholipase C ()

The GTP binding Gαh (transglutaminase II) mediates the α1B-adrenoreceptor signal to a 69-kDa phospholipase C (PLC). Thus, Gαh possesses both GTPase and transglutaminase activities with a signal transfer role. The recognition sites of this unique GTP binding protein for either the receptor or the eff...

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Bibliographic Details
Published in:The Journal of biological chemistry 1995-11, Vol.270 (45), p.27058-27062
Main Authors: Hwang, Ki-Chul, Gray, Caroline D., Sivasubramanian, Natarajan, Im, Mie-Jae
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Binding Sites - genetics
DNA Primers - genetics
DNA, Complementary - genetics
Guanosine Triphosphate - metabolism
Humans
In Vitro Techniques
Molecular Sequence Data
Myocardium - enzymology
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Sequence Deletion
Signal Transduction
Transglutaminases - genetics
Transglutaminases - metabolism
Type C Phospholipases - metabolism
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Summary:The GTP binding Gαh (transglutaminase II) mediates the α1B-adrenoreceptor signal to a 69-kDa phospholipase C (PLC). Thus, Gαh possesses both GTPase and transglutaminase activities with a signal transfer role. The recognition sites of this unique GTP binding protein for either the receptor or the effector are completely unknown. A site on human heart Gαh (hhGαh) has been identified that interacts with and stimulates PLC. Expressed mutants of hhGαh with deleted C-terminal regions lost the response to(-)-epinephrine and GTP and failed to coimmunoprecipitate PLC by the specific Gh7α antibody. The interaction regions were further defined by studies with synthetic peptides of hhGαh and a chimera in which residues Val665-Lys672 of hhGαh were substituted with Ile707-Ser714 residues of human coagulation factor XIIIa. Thus, eight amino acid residues near the C terminus of hhGαh are critical for recognition and stimulation of PLC.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.270.45.27058