Shed gangliosides provide detergent-independent evidence for type-3 glycosynapses |
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Authors: | Thorne Rick F Mhaidat Nizar M Ralston Kylie J Burns Gordon F |
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Institution: | Cancer Research Unit, School of Biomedical Sciences, The University of Newcastle, NSW, Australia. Rick.Thorne@newcastle.edu.au |
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Abstract: | Membrane microdomains, or rafts, at the plasma membrane have been invoked to explain many cellular processes. Protein-protein interactions within such microdomains including, for example, the tetraspanin web are reported to provide a scaffold for signal transduction. However, the nature of such protein-protein interactions is not fully elucidated. Hakomori S.I. Hakomori, The glycosynapse, Proc. Natl. Acad. Sci. USA 99 (2002) 225-232] has advanced the concept that glycosphingolipids, particularly gangliosides, provide the intermediary link between transmembrane receptors and signal transducers and has redefined membrane rafts as Type-1, -2 or -3 glycosynapses. Here, using simple immunofluorescent analysis of the ganglioside complexes naturally released from cellular microprocesses (termed "footprints") we show that the ganglioside can determine the nature of protein-protein associations. Specifically, we demonstrate that CD36 and the tetraspanin CD151, both of which interact with beta1 integrins, associate together only in the presence of the gangliosides GD2/GD3. These results substantiate the glycosynapse hypothesis and suggest that the nature of the tetraspanin web may be determined by gangliosides. |
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Keywords: | Ganglioside Tetraspanin web Glycosynapse Footprints |
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