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DISPLAYTITLE:Gi alpha subunit Gi protein alpha subunit is a family of heterotrimeric G protein alpha subunits. This family is also commonly called the Gi/o (Gi /Go ) family or Gi/o/z/t family to include closely related family members. G alpha subunits may be referred to as Gi alpha, Gαi, or Giα. There are four distinct subtypes of alpha subunits in the Gi/o/z/t alpha subunit family that define four families of heterotrimeric G proteins: Gi proteins: Gi1α, Gi2α, and Gi3α Go protein: Goα (in mouse there is alternative splicing to generate Go1α and Go2α) Gz protein: Gzα Transducins (Gt proteins): Gt1α, Gt2α, Gt3α Gi1α is encoded by the gene GNAI1. Gi2α is encoded by the gene GNAI2. Gi3α is encoded by the gene GNAI3. Go1α is encoded by the gene GNAO1. Gzα is encoded by the gene GNAZ. Transducin Transducin/Gt1α is encoded by the gene GNAT1. Transducin 2/Gt2α is encoded by the gene GNAT2. Gustducin Gustducin/Gt3α is encoded by the gene GNAT3. Heterotrimeric G protein The general function of Gi/o/z/t is to activate intracellular signaling pathways in response to activation of cell surface G protein-coupled receptors (GPCRs). GPCRs function as part of a three-component system of receptor-transducer-effector. The transducer in this system is a heterotrimeric G protein, composed of three subunits: a Gα protein such as Giα, and a complex of two tightly linked proteins called Gβ and Gγ in a Gβγ complex. When not stimulated by a receptor, Gα is bound to GDP and to Gβγ to form the inactive G protein trimer. When the receptor binds an activating ligand outside the cell (such as a hormone or neurotransmitter), the activated receptor acts as a guanine nucleotide exchange factor to promote GDP release from and GTP binding to Gα, which drives dissociation of GTP-bound Gα from Gβγ. GTP-bound Gα and Gβγ are then freed to activate their respective downstream signaling enzymes. Gi proteins primarily inhibit the cAMP dependent pathway by inhibiting adenylyl cyclase activity, decreasing the production of cAMP from ATP, which, in turn, results in decreased activity of cAMP-dependent protein kinase.

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