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Ubiquitylation of the chemokine receptor CCR7 enables efficient receptor recycling and cell migration

Ubiquitylation of the chemokine receptor CCR7 enables efficient receptor recycling and cell migration

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Prüfsumme: MD5:098e708e4cfc6b07e3179ab7353ca2d0

SCHÄUBLE, Karin, Mark A. HAUSER, Alexandra RIPPL, Roland BRUDERER, Carolina OTERO, Marcus GRÖTTRUP, Daniel F. LEGLER, 2012. Ubiquitylation of the chemokine receptor CCR7 enables efficient receptor recycling and cell migration. In: Journal of Cell Science. 125(19), pp. 4463-4474. ISSN 0021-9533. eISSN 1477-9137. Available under: doi: 10.1242/jcs.097519

@article{Schauble2012-10-01Ubiqu-21996, title={Ubiquitylation of the chemokine receptor CCR7 enables efficient receptor recycling and cell migration}, year={2012}, doi={10.1242/jcs.097519}, number={19}, volume={125}, issn={0021-9533}, journal={Journal of Cell Science}, pages={4463--4474}, author={Schäuble, Karin and Hauser, Mark A. and Rippl, Alexandra and Bruderer, Roland and Otero, Carolina and Gröttrup, Marcus and Legler, Daniel F.} }

Rippl, Alexandra Ubiquitylation of the chemokine receptor CCR7 enables efficient receptor recycling and cell migration deposit-license Hauser, Mark A. The chemokine receptor CCR7 is essential for lymphocyte and dendritic cell homing to secondary lymphoid organs. Owing to the ability to induce directional migration, CCR7 and its ligands CCL19 and CCL21 are pivotal for the regulation of the immune system. Here, we identify a novel function for receptor ubiquitylation in the regulation of the trafficking process of this G-protein-coupled seven transmembrane receptor. We discovered that CCR7 is ubiquitylated in a constitutive, ligand-independent manner and that receptor ubiquitylation regulates the basal trafficking of CCR7 in the absence of chemokine. Upon CCL19 binding, we show that internalized CCR7 recycles back to the plasma membrane via the trans-Golgi network. An ubiquitylation-deficient CCR7 mutant internalized normally after ligand binding, but inefficiently recycled in immune cells and was transiently retarded in the trans-Golgi network compartment of HEK293 transfectants. Finally, we demonstrate that the lack of CCR7 ubiquitylation profoundly impairs immune cell migration. Our results provide evidence for a novel function of receptor ubiquitylation in the regulation of CCR7 recycling and immune<br />cell migration. Bruderer, Roland eng 2012-10-01 Schäuble, Karin Hauser, Mark A. Journal of Cell Science ; 125 (2012), 19. - S. 4463-4474 Gröttrup, Marcus Rippl, Alexandra Schäuble, Karin 2013-03-12T16:13:21Z Legler, Daniel F. Bruderer, Roland Otero, Carolina Gröttrup, Marcus Otero, Carolina Legler, Daniel F. 2013-03-12T16:13:21Z

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

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