Guanylate-binding protein 2 (GBP2)

Guanylate-binding protein 2 (GBP2) is a member of the large GTPase superfamily, highly inducible by interferons such as interferon-gamma and involved in the innate immune response to intracellular pathogens[1][4][5][7]. GBP2 hydrolyzes GTP to GDP and undergoes nucleotide-dependent conformational changes that regulate its ability to dimerize, associate with cellular membranes, and interact with downstream effector proteins[1][4]. GBP2 is involved in modulating immune responses by restricting pathogen replication and has emerged as a key factor in the regulation of cellular processes such as mitochondrial dynamics, particularly via inhibition of Drp1-mediated mitochondrial fission. In cancer, especially breast cancer, GBP2 can suppress cell metastasis by blocking the mitochondrial recruitment of Drp1 and is associated with improved metastasis-free survival[2]. GBP2 is predominantly cytosolic but can associate with other organelles; its localization and function can be modulated by post-translational modification such as isoprenylation[7]. Its roles position GBP2 both as a biomarker and a potential (but not yet clinically targeted) therapeutic molecule in infection, cancer, and inflammation[2][5][7].

Other names

GBP2GBP-2HuGBP-2GTP-binding protein 2Guanine nucleotide-binding protein 2Interferon-induced guanylate-binding protein 2Guanylate binding protein 2, interferon-inducibleGuanylate-binding protein 2, GTP-binding protein 2

Not directly established for drugs, but mechanistic insight includes: inhibition of mitochondrial fission via Drp1 interaction and GTP hydrolysis-induced conformational changes affecting immune regulation