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| Name |
Bennett, Vann |
| Location
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Duke University Medical Center |
| Primary Field
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Physiology and Pharmacology |
| Secondary Field
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Cellular and Developmental Biology |
 Election Citation
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Bennett has advanced our molecular understanding of how membrane-spanning proteins connect to the cytoskeleton. His research revealed a family of proteins that mediate integral membrane protein attachments and clarified the roles of cell adhesion molecules in clinical disorders, including hemolytic anemia and cardiac arrhythmias. |
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Research Interests
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I have had a longstanding love affair with plasma membranes, beginning with my PhD research with Pedro Cuatrecasas. Postdoctoral training with Dan Branton introduced me to the human erythrocyte as a window into the world's simplest and most accessible plasma membrane. My laboratory used the erythrocyte model to discover ankyrin and its role in connecting the anion exchanger to the spectrin skeleton. We subsequently found that ankyrins and spectrins are ubiquitously expressed. Our laboratory has characterized ankyrins -B and -G and resolved their role in organization of a surprisingly diverse set of proteins and membrane domains. Ankyrins and their partners play pervasive roles in vertebrate physiology including recent evolutionary adaptations such as fast signaling in the nervous system and heart. We have determined a simple "code" for ankyrin-binding by membrane proteins, that has been independently accessed by many protein families. We have found that ankyrin proteins are required for both localization of membrane partners as well as for formation of specialized membrane domains including axon initial segments of neurons and lateral membrane domains of epithelial cells. We currently are exploring the molecular mechanisms underlying ankyrin function as well as the pathological consequences such as cardiac arrhythmia and diabetes when these mechanisms fail. |
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