Molecular interactions between dynamin and G-protein betagamma-subunits in neuroendocrine cells.
Dynamin and G-proteins both are guanosine triphosphate (GTP) binding proteins, with dynamin active in cellular membrane trafficking and G-proteins in intracellular signal transduction. Here we demonstrate that dynamin physically and functionally interacts with G-protein betagamma-subunits in neuroendocrine GH4C1 cells, on stimulation with thyrotropin-releasing hormone and somatostatin. The interaction appears to be of high affinity and inhibitory on dynamin GTPase activity, mediated by the pleckstrin homology domain and regulated both by the G-protein alpha-subunit and by guanosine nucleotides. Thus, dynamin may target particular sites for receptor-mediated endocytosis by sharing betagamma-subunits with the alpha subunit of G-proteins in neuroendocrine cells.
Liu
J P
JP
Department of Medical Oncology, Newcastle Mater Misericordiae Hospital, NSW, Australia. Jun-Ping.Liu@Baker.edu.au
Yajima
Y
Y
Li
H
H
Ackland
S
S
Akita
Y
Y
Stewart
J
J
Kawashima
S
S
D000818:Animals; D002460:Cell Line; D034281:Dynamins; D020558:GTP Phosphohydrolases / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000378:metabolism*; D009490:Neurosecretory Systems / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley; D015398:Signal Transduction
D020558:GTP Phosphohydrolases; D019204:GTP-Binding Proteins; D034281:Dynamins