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Originally published In Press as doi:10.1074/jbc.M202348200 on June 7, 2002

J. Biol. Chem., Vol. 277, Issue 41, 38700-38708, October 11, 2002
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Molecular Kinetics of Nerve Growth Factor Receptor Trafficking and Activation*

Jérôme JullienDagger §, Vincent GuiliDagger §, Louis F. Reichardt||**, and Brian B. RudkinDagger Dagger Dagger

From the Dagger  Differentiation and Cell Cycle Group, Laboratoire de Biologie Moleculaire et Cellulaire, CNRS UMR 5665, Ecole Normale Supérieure de Lyon, 46 Allée d'Italie, 69364 Lyon Cedex 07, France and the || Howard Hughes Medical Institute, University of California, San Francisco, California 94143

A growing body of evidence indicates a close relationship between tyrosine kinase receptor trafficking and signaling. Biochemical and molecular analyses of the expression, fate, and kinetics of membrane trafficking of the nerve growth factor (NGF) receptor TrkA were performed in PC12 cells. Pulse-chase experiments indicate that TrkA is synthesized as a 110-kDa N-glycosylated precursor that leads to the mature 140-kDa form of the receptor with a half-life of conversion of ~24 ± 0.5 min. Neuraminidase digestion shows that modification of the carbohydrate moiety of the receptor by sialylation occurs during maturation. The 140-kDa form is rapidly translocated to the cell surface as assessed by cell surface biotinylation performed on intact PC12 cells. Mature receptor half-life is ~138 ± 4 min and is shortened to 86 ± 8 min by NGF treatment. Flow cytometric analysis indicates that NGF induces clearing of this receptor from the cell surface within minutes of treatment. The addition of NGF decreases the half-life of cell surface gp140TrkA from 100 to 35 min and leads to enhanced lysosomal degradation of the receptor. The process of NGF-induced TrkA internalization is clearly affected by interfering with ligand binding to p75NTR. An analysis of receptor activation kinetics also shows that receptor signaling primarily takes place from an intracellular location. Together, these data show that the primary effect of NGF treatment is a p75NTR-modulated decrease in TrkA transit time at the cell surface.

* This work was supported by grants from the Ligue Nationale Contre le Cancer, the committee of the Ligue from the Rhône, the Rhône-Alpes Region, the Association for Research against Cancer (ARC), and the Fondation de France.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.

§ Supported by grants from the Ministère de l'Enseignement Supérieur et de la Recherche.

Recipient of fellowships from the Association for Research against Cancer.

** Investigator of the Howard Hughes Medical Institute. Work in his lab was supported by United States Public Health Service Grant NS 16033.

Dagger Dagger To whom correspondence should be addressed. Tel.: 334-7272-8196; Fax: 334-7272-8080; E-mail: bbrudkin@ens-lyon.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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