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G proteins, also known as guanine nucleotide-binding proteins, are a family of proteins that act as molecular switches inside cells, and are involved in transmitting signals from a variety of stimuli outside a cell to its interior.
G proteincoupled receptors (GPCRs) modulate the activity of many key metabolic functions that regulate glucose and energy homeostasis (1, 2). Metabolically relevant tissues and cell types express dozens of different GPCRs endowed with distinct G protein coupling properties (see below) (3).
DnaG is a bacterial DNA primase and is encoded by the dnaG gene. The enzyme DnaG, and any other DNA primase, synthesizes short strands of RNA known as oligonucleotides during DNA replication. These oligonucleotides are known as primers because they act as a starting point for DNA synthesis.
The primary function of G Proteins in signal transduction is: Transducting the signal from an activated receptor to the next protein in the pathway.
Inositol-requiring enzyme 1 (IRE1, also named ERN1) is an endoplasmic reticulum (ER)-resident transmembrane protein acting as a proximal sensor of the unfolded protein response (UPR).
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