The composition of protein aggregates affects their autophagy degradation efficiency and specificity.

On August 14th, Zhang Hong of the Institute of Biophysics of the Chinese Academy of Sciences published a research paper entitled The composition of a protein aggregate modulates the specificity and efficiency of its autophagic degradation in the journal Autophagy, which explains how the composition of protein aggregates affects their autophagy degradation efficiency and specificity.
autophagy (autophagy) is a common process of substance degradation and reuse of lysogen-mediated substances in gyrogenic organisms.
cells wrap "goods" by autophagy bodies that form a double-layer membrane structure and transport them to lysoes for degradation.
autophagy selectively degrades toxic protein aggregates to maintain the body's steady state balance.
autophagy abnormalities lead to the accumulation of these protein aggregates, which are associated with the development of a variety of diseases.
, however, the efficiency and specific mechanism of autophagy-degrading protein aggregates remain unclear.
early stage of the study, it was found that the PGL particles PGL-1 and PGL-3 (cargo) were selectively degraded by autophagy during the embryonic development of the Sully Cryptosomiasis.
further studies have found that the degradation process of P-particles is mediated by the receptor protein SEPA-1 (receptor) and the stent protein EPA-2 (scaffold), and that the receptor protein SEPA-1 and stent protein EPA-2 are eventually self-degraded.
, researchers studied the effects of PGL particle composition on autophagy degradation efficiency.
study found that the absence of PGL-1 and PGL-3 can promote the degradation of SEPA-1 and EPA-2, and the absence of EPA-1 can promote the degradation of EPA-2.
they also studied the relationships between different types of protein aggregates and found that the expression of PGL particles or SQST-1 (p62 congeners in worms) aggregations did not have a significant effect on another type of protein aggregation.
these phenomena, the researchers believe that the degradation of protein aggregates is affected by the group and is regulated at various levels.
Zhang Hong is the author of this article.
Zhang Hong, Ph.D., and Ph.D. student Lin Yu, co-author of this paper.
was funded by the National Natural Science Foundation of China, the Ministry of Science and Technology's Major Scientific Research Program (973) and the Howard Hughes Institute of Medicine's Young Scientists Fund.
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