Status: Bibliographieeintrag
Standort: ---
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| Online-Ressource |
Verfasst von: | Thelen, Karsten [VerfasserIn]  |
| Zelina, Pavol [VerfasserIn]  |
| Pollerberg, G. Elizabeth [VerfasserIn]  |
Titel: | Ubiquitination and endocytosis of cell adhesion molecule DM-GRASP regulate its cell surface presence and affect its role for axon navigation |
Verf.angabe: | Karsten Thelen, Tanja Georg, Stefanie Bertuch, Pavol Zelina, and G. Elisabeth Pollerberg |
Umfang: | 10 S. |
Fussnoten: | Gesehen am 09.05.2017 |
Titel Quelle: | Enthalten in: The journal of biological chemistry |
Jahr Quelle: | 2008 |
Band/Heft Quelle: | 283(2008), 47, S. 32792-32801 |
ISSN Quelle: | 1083-351X |
Abstract: | DM-GRASP, cell adhesion molecule of the immunoglobulin superfamily, has been shown to promote growth and navigation of axons. We here demonstrate that clustering of DM-GRASP in the plasma membrane induces its rapid internalization via dynamin- and clathrin-dependent endocytosis, which is controlled by phosphatidylinositol 3-kinase and mitogen-activated protein kinase ERK. The clustering of DM-GRASP activates ERK; the intensity and duration of ERK activation by DM-GRASP do not depend on rapid clathrin-mediated internalization of DM-GRASP. Moreover, the preference of retinal ganglion cell axons for DM-GRASP-coated micro-lanes requires clathrin-mediated endocytosis for the appropriate axonal turning reactions at substrate borders. Because the intracellular domain of DM-GRASP does not contain motifs for direct interactions with the endocytosis machinery, we performed a yeast two-hybrid screen to identify intracellular proteins mediating the uptake of DM-GRASP and isolated ubiquitin. Immunoprecipitation of DM-GRASP coexpressed with ubiquitin revealed that one or two ubiquitin(s) are attached to the intracellular domain of cell surface-resident DM-GRASP. Furthermore, elevated ubiquitination levels result in a decrease of cell surface-resident DM-GRASP as well as in the amount of total DM-GRASP. The endocytosis rate is not affected, but the delivery to multivesicular bodies is increased, indicating that DM-GRASP ubiquitination enhances its sorting into the degradation pathway. Together, our data show that ubiquitination and endocytosis of DM-GRASP in concert regulate its cell surface concentration, which is crucial for its function in axon navigation. |
DOI: | doi:10.1074/jbc.M805896200 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Kostenfrei: Verlag: http://dx.doi.org/10.1074/jbc.M805896200 |
| Kostenfrei: Verlag: http://www.jbc.org/content/283/47/32792 |
| DOI: https://doi.org/10.1074/jbc.M805896200 |
Datenträger: | Online-Ressource |
Sprache: | eng |
K10plus-PPN: | 1558342575 |
Verknüpfungen: | → Zeitschrift |
Ubiquitination and endocytosis of cell adhesion molecule DM-GRASP regulate its cell surface presence and affect its role for axon navigation / Thelen, Karsten [VerfasserIn] (Online-Ressource)
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