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Science 25 August 2000:
Vol. 289. no. 5483, pp. 1360 - 1365
DOI: 10.1126/science.289.5483.1360
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Reports

Regulated Cleavage of a Contact-Mediated Axon Repellent

Mitsuharu Hattori,* Miriam Osterfield, John G. Flanagandagger

Contact-mediated axon repulsion by ephrins raises an unresolved question: these cell surface ligands form a high-affinity multivalent complex with their receptors present on axons, yet rather than being bound, axons can be rapidly repelled. We show here that ephrin-A2 forms a stable complex with the metalloprotease Kuzbanian, involving interactions outside the cleavage region and the protease domain. Eph receptor binding triggered ephrin-A2 cleavage in a localized reaction specific to the cognate ligand. A cleavage-inhibiting mutation in ephrin-A2 delayed axon withdrawal. These studies reveal mechanisms for protease recognition and control of cell surface proteins, and, for ephrin-A2, they may provide a means for efficient axon detachment and termination of signaling.

Department of Cell Biology and Program in Neuroscience, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
*   Present address: Department of Molecular Neurobiology, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo, Japan.

dagger    To whom correspondence should be addressed. E-mail: flanagan{at}hms.harvard.edu

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   Abstract »    Full Text »    PDF »
Biochemical and Pharmacological Criteria Define Two Shedding Activities for TRANCE/OPGL That Are Distinct from the Tumor Necrosis Factor alpha Convertase.
J. Schlondorff, L. Lum, and C. P. Blobel (2001)
J. Biol. Chem. 276, 14665-14674
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Science. ISSN 0036-8075 (print), 1095-9203 (online)