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Membrane fusion mediated by ricin and viscumin
P Pohl1, Y N Antonenko, V Y Evtodienko
1Martin Luther Universität, Medizinische Fakultät, Institut für Medizinische Physik und Biophysik, 06097 Halle, Germany. peter.pohl@medizin.uni-halle.de
Biochimica Et Biophysica Acta
|May 30, 1998
Summary
Certain ribosome inactivating plant proteins (RIPs) like ricin can fuse vesicles, potentially explaining their toxicity by enabling escape into the cytoplasm to reach ribosomes.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Ribosome inactivating plant proteins (RIPs) are toxins that inhibit protein synthesis.
- The mechanism by which RIPs enter the cytoplasm to reach ribosomes is not fully understood.
- Vesicle fusion is a critical cellular process involved in transport and signaling.
Purpose of the Study:
- To investigate the ability of RIPs to induce vesicle-vesicle fusion.
- To explore the relationship between RIP fusogenicity and toxicity.
- To propose a model for RIPs' cellular entry and ribosome access.
Main Methods:
- Comparative analysis of ricin, viscumin, and Ricinus communis agglutinin.
- Assays to detect and quantify vesicle-vesicle fusion.
- Correlation of fusion activity with protein toxicity.
Main Results:
- Ricin and viscumin, but not Ricinus communis agglutinin, induced vesicle-vesicle fusion.
- A correlation was observed between the fusogenic potential of RIPs and their toxicity.
- Fusion is proposed as a mechanism for RIPs to cross endocytic vesicle membranes.
Conclusions:
- The fusogenicity of RIPs contributes to their toxicity.
- Vesicle fusion facilitates the translocation of RIPs from endocytic vesicles into the cytoplasm.
- This mechanism provides a pathway for RIPs to access and inhibit cytoplasmic ribosomes.