SGTA (small glutamine rich tetratricopeptide repeat co-chaperone alpha) functions as a molecular co-chaperone involved in protein quality control and cellular proteostasis 1. The protein collaborates with the BAG6 complex to facilitate biogenesis and quality control of hydrophobic proteins, including targeting tail-anchored proteins to membranes and participating in endoplasmic reticulum-associated degradation of misfolded proteins 1. SGTA contains an N-terminal dimerization domain that forms tight dimeric structures, a central tetratricopeptide repeat (TPR) domain, and a C-terminal glutamine-rich region 2. The protein interacts with molecular chaperones HSP70 and HSP90, and serves as a negative modulator of androgen receptor signaling through interference with dynein-dependent transport 34. Clinically, SGTA overexpression correlates with poor prognosis in hepatocellular carcinoma and breast cancer, where it promotes cell proliferation through regulation of cyclins A and B 56. Additionally, SGTA associates with protein aggregates in neurodegenerative diseases including polyglutamine diseases and multiple system atrophy, potentially modulating aggregate formation 7. The protein also interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism, linking it to protein degradation pathways 8.