Functions of SGT1, a Co-chaperone

  • Yohei NiikuraEmail author
  • Katsumi KitagawaEmail author
Part of the Heat Shock Proteins book series (HESP, volume 19)


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.


Brain and heart diseases Cancer E3 ubiquitin ligase Kinetochore Post-translational modification (PTM) SGT1/SUGT1 





Adenylyl cyclase


Amyotrophic lateral sclerosis


Centromere binding factor 3


Calcium-dependent protein kinase


Centromere protein-A


Centromere protein-B


Cysteine- and histidine-rich domain


Comparative Proteomic Analysis Software Suite


CHORD protein and SGT1-specific




Cell wall protein


Dilated cardiomyopathy


Eukaryotic elongation factor 1




Hypersensitive response


Heat shock protein




Interleukin 1


Leucine rich repeats


Monosodium urate


Nuclear factor kappa-light-chain-enhancer of activated B cells


Nucleotide binding leucine-rich repeat receptor


Nucleotide-binding oligomerization domain


Pathogen-associated molecular pattern


Programmed cell death






Polo-like kinase


Protein quality control


Post-translational modification

R proteins

Resistance proteins


Required for Mla12 resistance

S. cerevisiae

Saccharomyces cerevisiae


SKP1, Cullin, F-box




Suppressor of G2 allele of SKP1


Tumor necrosis factor alpha


Tetratricopeptide repeat


Ubiquitin-protein ligase E3A


Ubiquitin-dependent 26S proteasome system



We thank past and current researchers at Greehey Children’s Cancer Research Institute at UT Health Science Center San Antonio School of Medicine, The Research Institute at Nationwide Children’s Hospital, and St. Jude Children’s Research Hospital for their helpful discussions. This work was supported by NCI R21CA205659 and institutional support from Greehey Children’s Cancer Research Institute and MOE Key Laboratory of Model Animal for Disease Study, Model Animal Research Center, Nanjing University.


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© Springer Nature Switzerland AG 2019

Authors and Affiliations

  1. 1.MOE Key Laboratory of Model Animal for Disease Study, Model Animal Research CenterNanjing UniversityNanjing, Jiangsu ProvinceChina
  2. 2.Greehey Children’s Cancer Research Institute, Department of Molecular MedicineUT Health San AntonioSan AntonioUSA

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