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Figure 10


Fig. 10. Model for laminin-1-induced clustering of GM-1, TrkA, β1 integrin and signaling molecules in lipid rafts required for neurite outgrowth. Laminin-1 directly binds to GM1 and induces its focal aggregation, thereby enhancing the relocation of TrkA in the lipid rafts and the subsequent activation of NGF-signaling molecules such as Lyn. Clustering of GM1 with laminin-1 also promotes relocation and enrichment of β1 integrin in lipid rafts, and enhances the combined laminin-1–integrin signaling of laminin-1 and integrins. Laminin-1 self-assembly might stabilize and enhance the focal formation of the GM1-enriched microdomain in the membrane. The focal lipid-raft structure enriched with TrkA, integrin and signaling molecules provides a functional platform within the membrane that helps to link and activate NGF-TrkA and laminin-1–integrin signaling pathways that trigger neurite outgrowth in a cooperative manner.





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