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The SGTA is a co-chaperone that, in collaboration with the complex of BAG6, facilitates the biogenesis and quality control of hydrophobic proteins, protecting them from the aqueous cytosolic environment.
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the results provide novel insights into the structural complexity of SGTA and provide a new basis for mechanistic studies of substrate binding and release at the C-terminal region.
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evidence that the interaction can mediate the association of Rpn13 and SGTA in a cellular context.
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Coimmunoprecipitation studies indicated that non-glycosylated tetherin is stabilized through the formation of a ternary SGTA/Vpu/tetherin complex. Although the results do not provide support for a physiological function of SGTA in HIV-1 replication, they demonstrate that SGTA overexpression regulates tetherin expression and stability, thus providing insights into the function of SGTA in endoplasmic reticulum translocation
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study demonstrates a critical role of Hsc70 in SV40 endoplasmic reticulum-to-cytosol penetration and reveal how SGTA controls Hsc70 to impact this process
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the binding of SGTA to Rpn13 enables specific polypeptides to escape proteasomal degradation and/or selectively modulates substrate degradation.
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data suggest that SGTA regulates the cellular fate of a range of hydrophobic polypeptides should they become exposed to the cytosol.
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Data show that molecular chaperone BAG6_ubiquitin-like domain (UBL) and ubiquitin-like 4A UBL4A_UBL compete for the same binding site on N-terminal dimerisation domain of SGTA protein (SGTA_NT).
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SGTA overexpression may be involved in the pathogenesis of breast cancer which might serve as a future target for novel treatment in breast cancer.
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Our data suggest a role for SGTA at distinct steps in the chaperone-dependent modulation of androgen, glucocorticoid, and progesterone receptor activity.
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SGTA depletion decreased cyclin A and cyclin B levels.
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A role of SGTA in Non-Hodgkin's lymphoma (NHL) cell proliferation, adhesion and drug resistance, and it may pave the way for a novel therapeutic approach for cell adhesion-mediated drug resistance in NHL.
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High expression of SGTA in esophageal squamous cell carcinoma correlates with proliferation and poor prognosis.
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Univariate analysis showed that the low SGTB expression was associated with poor prognosis (P<0.001)
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showed a significant increase in the AR:SGTA ratio in cancerous lesions compared to patient-matched benign prostatic hyperplasia tissue
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High Small glutamine-rich tetratricopeptide repeat-containing protein alpha expression is associated with non-small-cell lung cancer tumorigenesis.
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SGTA is present in human ovaries and has the potential to modulate androgen receptor signalling, but it may not be differentially expressed in polycystic ovary syndrome.
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SGTA recognizes a noncanonical ubiquitin-like domain in the Bag6-Ubl4A-Trc35 complex to promote endoplasmic reticulum-associated degradation.
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Structures of the Sgt2/SGTA dimerization domain with the Get5/UBL4A UBL domain reveal an interaction that forms a conserved dynamic interface.
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Homodimerizaion of SGTA is dependent on the structural integrity of amino acids 1-80, and a core evolutionary conserved peptide within this region (amino acids 21-40) necessary for an effect of SGTA on the activity of the androgen receptor.