Whether a sick cell dies, divides, or travels through the body is regulated by a sophisticat-ed interplay of signal molecules and receptors on the cell membrane. One of the most im-portant molecular cues in the immune system is Tumour Necrosis Factor α (TNFα).
Now, for the first time, researchers from Goethe University have visualised the molecular organization of individual TNFα receptor molecules and the binding of TNFα to the cell mem-brane in cells using optical microscopy.
Before TNFα can bind to a membrane receptor, the TNFR receptor must first be activated. By doing so, the key will only fit the lock under certain circumstances and prevents, among other things, that a healthy cell dies from programmed cell death.
For TNFR1 in the membrane, the binding of TNFα is mediated through several cysteine-rich domains, or CRDs." Sjoerd van Wijk, Institute for Experimental Cancer Research in Paediatrics and Frankfurt Stiftung für Krebskranke Kinder, Goethe University
In particular, CRD1 of the TNFR1 makes it possible for TNFα to "attach". Researchers already knew that TNFR1 molecules cluster in a fashion similar to a dance, in which two, three or more partners grasp hands - with the dimers, trimers or oligomers consisting of single TNFR1 mole-cules - in the case of TNFR1. This kind of "structural reorganization" also takes place when there is no TNFα present. "Despite the significance of TNFα for many diseases, including in-flammation and cancer, the physiology and patterns of TNFR1 in the cell membrane still remain largely unknown up to now," says Sjoerd Van Wijk, explaining the starting point for his research. Related Stories
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