Jump to ContentJump to Main Navigation

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

12 Issues per year

IMPACT FACTOR increased in 2014: 3.268
Rank 106 out of 289 in category Biochemistry & Molecular Biology in the 2014 Thomson Reuters Journal Citation Report/Science Edition

SCImago Journal Rank (SJR) 2014: 1.596
Source Normalized Impact per Paper (SNIP) 2014: 0.845
Impact per Publication (IPP) 2014: 2.992



Signal Transduction by the Chemokine Receptor CXCR5: Structural Requirements for G Protein Activation Analyzed by Chimeric CXCR1/CXCR5 Molecules

G. Müller / M. Lipp

Citation Information: Biological Chemistry. Volume 382, Issue 9, Pages 1387–1397, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2001.171, June 2005

Publication History

Published Online:


The human chemokine receptors CXCR5 and CXCR1 activate signaling pathways via pertussis toxinsensitive as well as insensitive G proteins. CXCR5 induces Ca2+signaling and chemotaxis independently of inhibitory G proteins, whereas the same signaling pathways are entirely dependent on inhibitory G proteins for CXCR1. In contrast, activation of the MAP kinase cascade via ERK1/2 is a pertussis toxinsensitive signaling event for both receptors. Using chimeric CXCR1/CXCR5 receptors we investigated structural requirements for the activation of signal transduction pathways by CXCR5. Individual or multiple intracellular domains of CXCR1 were exchanged for the corresponding sequences of CXCR5, leading to receptors resembling CXCR5 at the cytoplasmic surface to a varying extent. Replacing the second intracellular domain of CXCR1 had a major influence on signaling mediated by inhibitory G proteins, whereas the exchange of the third or carboxyterminal intracellular domain had only minor effects on signal transduction. Activation of the MAP kinase cascade via ERK1/2 and chemotaxis are largely reduced in chimeras comprising the second intracellular domain of CXCR5, although coupling to inibitory G proteins is retained in all chimeric receptors. In summary, these data characterize the contribution of the intracellular domains of CXCR5 to receptor signaling, thereby disclosing unique structural requirements that modulate G protein coupling by the receptor.

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

Ana Costa, Alix Scholer-Dahirel, and Fatima Mechta-Grigoriou
Seminars in Cancer Biology, 2014, Volume 25, Page 23
Henrik Flach, Marc Rosenbaum, Marlena Duchniewicz, Sola Kim, Shenyuan L. Zhang, Michael D. Cahalan, Gerhard Mittler, and Rudolf Grosschedl
Immunity, 2010, Volume 33, Number 5, Page 723
J. P. Pereira, L. M. Kelly, and J. G. Cyster
International Immunology, 2010, Volume 22, Number 6, Page 413
N Thirunarayanan, F Cifire, I Fichtner, S Posner, J Benga, P Reiterer, E Kremmer, K Kölble, and M Lipp
Oncogene, 2007, Volume 26, Number 39, Page 5702

Comments (0)

Please log in or register to comment.