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Second, we examine selective protein quality control, in which SGPA identifies most known quality control factors along with U34 tRNA modification, which acts independently of proteasomal degradation to limit misfolded protein production.
Because cytoplasmic ssDsbA-sfGFP folds very rapidly and is resistant to unfolding, it is likely that cellular quality control factors (e.g., proteases) are unable to eliminate this protein and it accumulates in a fluorescent conformation.
The HSR is induced by the accumulation of misfolded proteins within the cytosol, resulting in the activation of stress-responsive transcription factors that induce transcriptional programs including proteostasis network components such as chaperones, cochaperones, folding enzymes, and quality control factors.
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In S. cerevisiae it also contains three phosphorylation sites that are important for binding to the proteasome quality control factor, Ecm29 (Wani et al., 2016).
It seems therefore relevant to establish the role of the lectin site of Malectin for the in vivo function of this novel ER-resident quality control factor.
TAp63α, a homolog of the p53 tumor suppressor, is a quality control factor in the female germline.
Monitoring the screening interval is an important quality control factor for increasing the detection of tumors at an early stage.
The TAp63α isoform, lacking some of its carboxyl terminus, serves as a quality control factor in the female germ line.
In oocytes, TAp63 α is responsible for DNA damage-induced apoptosis, therefore functioning as a quality control factor in the female germline.
It is found in oocytes where it acts as a quality control factor that monitors the genetic stability of these cells (Suh et al., 2006).
In oocytes, TAp63 α expresses at relatively higher levels and functions as a quality control factor in the female germline, upon genotoxic stress [ 21– 23].
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