研究领域

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Cues in the extracellular microenvironment govern the behavior of migrating cells by triggering changes in migration speed or direction. The cell surface receptors that interpret these cues engage cytoplasmic partners to transduce signals, but recent work reveals that many receptors also interact laterally with cell surface proteins that can be critical for proper receptor function. Thus, a more sophisticated understanding of cell migration will require a "cell surface interaction map" describing the physical and functional connections between receptors and their cell surface partners. To begin to build such an interaction map, we have initially focused on integrins, the major receptors for extracellular matrix proteins. Integrins mediate cell adhesion and migration during development, in homeostasis, and in a variety of pathological settings, including tumor cell metastasis. Integrins are heterodimers composed of one α and one β subunit. While both subunits contribute to ligand-binding specificity, the β subunit cytoplasmic tail mediates most of the established integrin signaling and cytoskeletal interactions that have been identified. Thus at present there is no satisfactory explanation for how different integrins that share a common β subunit are able to mediate different cellular responses. For example, tumor cell motility mediated by α3β1 integrin on its ligand, laminin-332 (laminin-5), can be 3-4 fold faster than motility mediated by other β1 integrins, such as the collagen receptor, α2β1, or the fibronectin receptor, α5β1.

Cell and Developmental Biology, Neurobiology