Vance Lemmon , Ph.D.

Walter G. Ross Chair in Developmental Neuroscience

Miami Project to Cure Paralysis

Professor of Neurological Surgery

Lois Pope LIFE Center, Room 4-16
1095 NW 14th Terrace
Miami, Florida 33136
Telephone: 305-243-6793
FAX: 305-243-3921

e-mail: vlemmon@miami.edu

Vance Lemmon Lab Web Site




Curriculum Vitae:
B.A. 1973 Biology, Revelle College, UCSD
Ph.D. 1978 Anatomy, Emory University
Postdoctorate 1978-1981 Neurobiology (with Alan Pearlman and David Gottlieb), Washington University, St. Louis, MO
Assistant Professor 1981-1983 Anatomy, MUSC, Charleston, SC
Assistant Professor 1983-1988 Neurobiology, University of Pittsburgh
Associate Professor 1988-1995 Neurosciences, CWRU, Cleveland, OH
Professor 1995-2003 Neurosciences, CWRU, Cleveland, OH
Professor 2003-present Neurological Surgery, University of Miami


Research Interests:

L1 is a neural cell adhesion molecule of the Ig superfamily. It was identified independently in the 1970's and 1980's by several labs, mostly by people making monoclonal antibodies to neural tissue. It's most striking feature is its strong expression on axons in the CNS and PNS. Early cell culture experiments from different labs indicated that L1 was involved in axon growth. In 1987 Carl Lagenaur and I showed that purified L1 was a potent promoter of axon growth. These observations have led many investigators to study L1 in development and in nerve regeneration. Indeed it has been implicated in a variety of systems and processes, including neural cell migration, learning and neural plasticity. The discovery that mutations in the L1 gene caused X-linked hydrocephalus, confirmed the importance of L1 for brain development. As a result, along with NCAM, L1 is one of the best studied neural CAMs.

For the past 10 years my lab has focused on understanding how the L1 cytoplasmic domain is involved in L1 function. We are convinced that L1 is not simply a passive sticky material that glues axons together or to other cells. Rather it has important signaling properties critical for axon growth and guidance. The L1 cytoplasmic domain binds to several cytoplasmic proteins that are critical in this process and these include cytoskeletal components and proteins involved in protein trafficking as well as kinases and phosphatases. Cell biological, biochemical and molecular studies are in progress to further our understanding of these phenomena.

At the Miami Project to Cure Paralysis we are also using advanced molecular biological approaches combined with in vivo experimentation to study how axons grow long distances through the adult central nervous system in the hopes of identifying molecules that can help promote regeneration in damaged spinal cords.


Selected Publications:

A.W. Schaefer, Y. Kamei, H. Kamiguchi, E.V. Wong, I. Rapoport, T. Kirchhausen, C.M. Beach, G. Landreth, S.K. Lemmon, V. Lemmon. (2002) L1 endocytosis is controlled by a phosphorylation-dephosphorylation cycle stimulated by outside-in signaling by L1. J. Cell Biology, 157:1223-1232.

De Angelis, E., Brümmendorf, T., Cheng, L., Lemmon, V., and Kenwrick, S. (2001) Alternative use of a mini exon of the L1 gene affects L1 binding to neural ligands. J. Biol. Chem., 276:32738-32742.

Long, K.E., Asou, H., Snider, M.D., Lemmon, V. (2001) The role of endocytosis in regulating L1-mediated adhesion. J.Biol.Chem., 276:1285-1290.

Kamiguchi, H., Long, K.E., Pendergast, M., Schaefer, A.W., Rapoport, I., Kirchhausen, T., Lemmon, V. (1998) The neural cell adhesion molecule L1 interacts with the AP-2 adaptor and is endocytosed via the clathrin-mediated pathway. J.Neurosci., 18:5311-5321.

 

Last updated August 28, 2003

 

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