G. Vann Bennett
Professor of Cell Biology and Biochemistry and Investigator, Howard Hughes Medical Institute
Biochemistry of spectrin-based membrane skeleton and other membrane skeletal proteins.
Contact Information
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Telephone: (919) 684-3538 Fax: (919) 684-3590 e-mail benne012@mc.duke.edu Carl Building |
Mailing Address Dr. Vann Bennett 365 Carl Building Box 3892, DUMC Durham NC 27710 |
Education
- Ph.D. (Johns Hopkins School of Medicine, 1974)
- M.D. (Johns Hopkins School of Medicine, 1976)
Research Interests
This laboratory has focused on a system of proteins associated with the cytoplasmic surface of plasma membranes of most animal cells known as the spectrin-based membrane skeleton. Spectrin and its associated proteins are candidates to play a role in local ization of integral membrane proteins at specialized regions of the plasma membrane. Examples of physiologically important cell domains involving spectrin include axons of neurons, the neuromuscular junction, nodes of Ranvier of myelinated axons, and baso lateral domains of epithelial cells. Our research has focused on basic questions related to association of spectrin skeleton. Much of the work involves ankyrin and adducin which are two spectrin-binding proteins discovered by this laboratory. Ankyrins are a family of spectrin-binding proteins that link the spectrin skeleton to multiple membrane proteins, including ion channels such as the voltage dependent sodium channel, and the Na/K ATPase. Adducin is a candidate to promote sitedirected assembly of spec trin at specialized regions of cell membranes, and is a major substrate for protein kinase C. Progress in the last year has resulted in the complete cloning and sequencing of cDNAs encoding both adducin subunits as well as of an unusual brain ankyrin high ly expressed in the neonatal period. In addition, a family of integral proteins have been discovered in brain that associates with brain ankyrin.
Recent Publications
1. P. A. Norton, T. Uporova and V. D. Bennett (1998) “A highly conserved region upstream of the fibronectin alternative exon EIIIA 3’ splice site interacts with cell-type-specific nuclear proteins.” Biochim Biophys Acta 2:145-50. More…
2. K. Kimura, Y. Fukata, Y. Matsuoka, V. Bennett, Y. Matsuura, K. Okawa, A. Iwamatsu and K. Kaibuchi (1998) “Regulation of the association of adducin with actin filaments by Rho- associated kinase (Rho-kinase) and myosin phosphatase.” J Biol Chem 10:5542-8. More…
3. Q. Ren and V. Bennett (1998) “Palmitoylation of neurofascin at a site in the membrane-spanning domain highly conserved among the L1 family of cell adhesion molecules.” J Neurochem 5:1839-49. More…
4. A. L. Gehris, E. Stringa, J. Spina, M. E. Desmond, R. S. Tuan and V. D. Bennett (1997) “The region encoded by the alternatively spliced exon IIIA in mesenchymal fibronectin appears essential for chondrogenesis at the level of cellular condensation.” Dev Biol 2:191-205. More…
5. V. Bennett and R. Lee (1997) “Modeling seasonal changes in intracellular freeze-tolerance of fat body cells of the gall fly eurosta solidaginis [In Process Citation].” J Exp Biol Pt 20:185-92. More…
6. S. Tuvia, T. D. Garver and V. Bennett (1997) “The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation.” Proc Natl Acad Sci U S A 24:12957-62. More…