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Published 12 November 2001. doi:10.1083/jcb1554iti3
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© The Rockefeller University Press, 0021-9525/2001/11/494 $5.00
The Journal of Cell Biology, Volume 155, Number 4, November 12, 2001 494-494

In This Issue

Cleaving and migrating


L1 helps cells migrate.

Aglycoprotein, more often thought of as an immobilized substrate for crawling over, can also be cleaved to form a soluble signal that promotes cell migration, according to Mechtersheimer et al. (page 661).

The glycoprotein L1 mediates axon guidance and cell migration in the nervous system. Mechtersheimer et al. find that L1 in newborn mouse brain and in certain tumor cells is cleaved. The soluble fragment promotes migration over several substrates, and transfection of CHO cells with an L1 construct enhances migration.

Based on inhibition studies and experiments with mutants, the authors suggest that the metalloproteinase ADAM10 cleaves L1, and the L1 fragment then binds integrins on the same or a nearby cell. Signaling downstream of the integrin probably acts as a general stimulus for migration. ADAM10 can also cleave certain growth factors, thus activating their signaling pathways, which may converge with the L1/ integrin pathway. As L1 and ADAM10 are widely expressed, the temporal and spatial regulation of L1 cleavage may involve as yet uncharacterized molecules. {blacksquare}



William A. Wells

wellsw{at}rockefeller.edu


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Related Article

Ectodomain shedding of L1 adhesion molecule promotes cell migration by autocrine binding to integrins
Sabine Mechtersheimer, Paul Gutwein, Nancy Agmon-Levin, Alexander Stoeck, Matthias Oleszewski, Svenja Riedle, Rolf Postina, Falk Fahrenholz, Mina Fogel, Vance Lemmon, and Peter Altevogt
J. Cell Biol. 2001 155: 661-674. [Abstract] [Full Text] [PDF]




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