Intracellular Transport of Ribosome-Inactivating Proteins Depends on Annexin 13
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HEMISTRY, BIOPHYSICS, AND MOLECULAR BIOLOGY
Intracellular Transport of Ribosome-Inactivating Proteins Depends on Annexin 13 D. V. Maltsevaa,b,c,*, M. P. Raigorodskayab, V. G. Zgodad, E. A. Tonevitskye, and E. N. Knyazeva,** Presented by Academician A.V. Lisitsa Received March 19, 2020; revised April 6, 2020; accepted April 6, 2020
Abstract– In the present study, we assessed the role of annexin 13 membrane-binding protein (ANXA13) in the intracellular transport of vesicles containing type II ribosome-inactivating proteins (RIP-IIs). A modified human intestinal epithelial cell line HT29 was used, in which the expression of ANXA13 was significantly reduced. The cytotoxic effect of ricin and viscumin was evaluated by modification of 28S ribosome RNA. The observed differences in the activity of toxins on the parental and modified HT29 lines indicate that ANXA13 plays a different role in the intracellular transport of vesicles containing the RIP-IIs. Keywords: ANXA13, HT29, MLI, annexin 13, endocytosis, intestinal epithelium, intracellular transport, ribosome-inactivating protein, ricin, viscumin DOI: 10.1134/S1607672920040092
Endocytosis, the mechanism of vesicular transport of various molecules from the plasma membrane of eukaryotic cells into the cytoplasm, is involved in a wide range of physiological processes [1]. In eukaryotic cells, several different pathways of endocytosis have been described. However, despite the long-term research, many details of this process remain unclear [1]. Type II ribosome-inactivating proteins (RIP-II) are a classic tool for identifying new and deeper understanding of already known pathways of intracellular transport [1, 2]. The widely used RIP-IIs include ricin and viscumin, which have the same mechanism of action and are structural homologs [2–4], but their cytotoxic activity significantly differs [5–8]. Both proteins consist of two chains, catalytic (A chain) and binding (B chain), which are connected through a disulfide bond. The B chain binds to glycosylated proteins and lipids containing the terminal galactose residue on the cell surface. Part of the RIP-II molecules bound to the membrane undergo endocytosis in coma Shemyakin-Ovchinnikov
Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia b Scientific Research Center Bioclinicum, Moscow, Russia c Faculty of Biology and Biotechnology, National Research University Higher School of Economics, Moscow, Russia d Institute of Biomedical Chemistry, Moscow, Russia e Development Fund of the Mendeleev Valley Innovation Science and Technology Center, Moscow, Russia *e-mail: [email protected] **e-mail: [email protected]
ponents of membrane vesicles and subsequent retrograde transport to the endoplasmic reticulum (ER), where the disulfide bond is reduced and the A chain is translocated to the cytoplasm. The A chain is an N-glycosidase and irreversibly modifies the ribosomal 28S RNA, which leads to termination of protein synthesis. An important feature of work with RIP-II is the possibility to quantify the prop
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