Here, we present a study of the interactions of cell membrane with multiple membrane signaling proteins including Plexin-B1 receptor, the EphA2 receptor and the Ras: Raf protein complex. We compare the similarities and differences between the membrane interactions of single-domain protein, multi-domain protein and multi-protein complexes. Separated domains of EphA2 could associate with the membrane in both a cooperative and a non-cooperative manner; while separated subunits of Ras: Raf complex only associate with the membrane in a competitive manner. Membrane interactions of the Plexin-B1 receptor limit the accessibility of membrane-anchored small GTPases (Rnd1/Rac1 and Rap1b). In all cases, the membrane interactions also has an influence on the internal dynamics of the proteins/protein domains. Taken together, the changes of the morphology and internal dynamics of protein or protein complex due to the membrane interactions play a role in directing effector protein recognition as well as protein self-assembly. Our studies highlight the role of the cell membrane as an active modulator of protein function.

Comparative study between membrane interactions of signal proteins Plexin-B1, EphA2 and the K-Ras Ras: Raf complex

2019 Spring National Meeting

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