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Originally published In Press as doi:10.1074/jbc.M006658200 on October 16, 2000

J. Biol. Chem., Vol. 276, Issue 2, 1285-1290, January 12, 2001
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The Role of Endocytosis in Regulating L1-mediated Adhesion*

Kristin E. LongDagger , Hiroaki Asou§, Martin D. Snider, and Vance LemmonDagger ||

From the Dagger  Department of Neurosciences and  Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio 44106 and § Department of Neurobiology, Tokyo Metropolitan Institute of Gerontology 35-2, Itabashi-ku, Tokyo, 173-0015, Japan

L1 is a neural cell adhesion molecule critical for neural development. Full-length L1 (L1FL) contains an alternatively spliced cytoplasmic sequence, RSLE, which is absent in L1 expressed in nonneuronal cells. The RSLE sequence follows a tyrosine, creating an endocytic motif that allows rapid internalization via clathrin-mediated endocytosis. We hypothesized that L1FL would internalize more rapidly than L1 lacking the RSLE sequence (L1Delta RSLE) and that internalization might regulate L1-mediated adhesion. L1 internalization was measured by immunofluorescence microscopy and by uptake of 125I-anti-rat-L1 antibody, demonstrating that L1FL is internalized 2-3 times faster than L1Delta RSLE. Inhibition of clathrin-mediated endocytosis slowed internalization of L1FL but did not affect initial uptake of L1Delta RSLE. To test whether L1 endocytosis regulates L1 adhesion, cell aggregation rates were tested. L1Delta RSLE cells aggregated two times faster than L1FL cells. Inhibition of clathrin-mediated endocytosis increases the aggregation rate of the L1FL cells to that of L1Delta RSLE cells. Our results demonstrate that rapid internalization of L1 dramatically affects L1 adhesion.

* This work was supported by National Institutes of Health Grants EY-05285 and P30EY11373 (to V. L.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Dept. of Neurosciences, Case Western Reserve University School of Medicine, Rm. E661, 2109 Adelbert Rd., Cleveland, OH 44106-4975. Tel.: 216-368-3039; Fax: 216-368-4650; E-mail vxl@po.cwru.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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