Signal activation and inactivation by the Gα helical domain: a long-neglected partner in G protein signaling.
Heterotrimeric guanine nucleotide-binding proteins (G proteins) are positioned at the top of many signal transduction pathways. The G protein α subunit is composed of two domains, one that resembles Ras and another that is composed entirely of α helices. Historically most attention has focused on the Ras-like domain, but emerging evidence reveals that the helical domain is an active participant in G protein signaling.
Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA. hdohlman@med.unc.edu
Henrik G
HG
Dohlman
Janice C
JC
Jones
D000818:Animals; D004789:Enzyme Activation / Q000502:physiology; D044385:GTP-Binding Protein alpha Subunits / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D015689:Oncogene Protein p21(ras) / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D015398:Signal Transduction / Q000502:physiology*
D044385:GTP-Binding Protein alpha Subunits; D015689:Oncogene Protein p21(ras)