SGTA


Description

The SGTA (small glutamine rich tetratricopeptide repeat co-chaperone alpha) is a protein-coding gene located on chromosome 19.

SGTA, also known as Small glutamine-rich tetratricopeptide repeat-containing protein alpha, is a protein found in humans and other mammals. It belongs to a family of co-chaperone proteins that contain a TPR motif and was discovered relatively recently, about 15 years ago. SGTA is involved in various cellular processes, including hormone signaling, viral assembly, cell cycle regulation, and protein trafficking. Its primary function is to act as a co-chaperone, helping to fold and transport proteins. SGTA has been shown to interact with various proteins, including growth hormone receptors, chaperone proteins HSC70 and HSP70, and the BAG6 complex. SGTA is essential for the proper folding and trafficking of proteins and plays a role in cellular responses to stress and viral infections.

SGTA acts as a co-chaperone, binding misfolded proteins in the cytosol and guiding them to the endoplasmic reticulum (ER). If targeting to the ER fails, SGTA helps direct these proteins to the proteasome for degradation. It plays a key role in the insertion of tail-anchored and type II transmembrane proteins into the ER membrane, working in concert with ASNA1 and the BAG6 complex. SGTA acts upstream of this complex, binding rapidly to newly synthesized proteins. SGTA interacts with BAG6 to regulate the breakdown of misfolded proteins in the ER, ensuring these proteins remain non-ubiquitinated. It competes with RNF126 for binding to BAG6, preventing the ubiquitination of client proteins associated with the BAG6 complex. SGTA directly interacts with HSC70 and HSP70, regulating their ATPase activity.

SGTA is also known as SGT, SGT1, Vpu, alphaSGT, hSGT.

Associated Diseases



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