SGT1/SUGT1, a co-chaperone of HSP90, is involved in multiple cellular activities including cullin E3 ubiquitin ligase activity. In various species, SGT1 homologs have been identified, indicating that SGT1 genes and proteins are highly conserved. SGT1 functions in multiple distinct biological processes, such as plant and mammal innate immune systems, yeast CBF3 kinetochore assembly, human CENP-A deposition and kinetochore assembly, SCF function and cyclic AMP signaling, centrosome organization and cytokinesis, and brain and heart diseases. Domain-specific functions, interactors, and roles in subcellular localization of SGT1 are described in this chapter. Importantly, SGT1 contributes to cancer development by stabilizing oncoproteins, and the SGT1-HSP90 complex is a potential target for therapies aimed at cancer, brain and heart disease. Recent advances in our understanding of the physiologic role of SGT1 are briefly reviewed in this chapter.
CITATION STYLE
Niikura, Y., & Kitagawa, K. (2019). Functions of SGT1, a Co-chaperone (pp. 317–370). https://doi.org/10.1007/978-3-030-23158-3_16
Mendeley helps you to discover research relevant for your work.