期刊
SCIENCE
卷 289, 期 5483, 页码 1360-1365出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.289.5483.1360
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资金
- NEI NIH HHS [EY11559] Funding Source: Medline
- NICHD NIH HHS [HD29417] Funding Source: Medline
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.
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