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 Previous Article | Table of Contents | Next Article 
 -Chemokine Receptor CCR5 Signals Via the Novel Tyrosine Kinase RAFTK
Ramesh K. Ganju,
Parmesh Dutt,
Lijun Wu,
Walter Newman,
Hava Avraham,
Shalom Avraham, and
Jerome E. Groopman
From the Divisions of Experimental Medicine and Hematology/Oncology,
Beth Israel Deaconess Medical Center, Harvard Medical School, Boston,
MA and LeukoSite, Inc, Cambridge, MA.
Chemokine receptors are coupled to G-proteins and their activation
results in prominent changes in cell migration and growth. The
downstream signaling pathways that mediate these effects of chemokines
are largely uncharacterized. Macrophage inflammatory protein 1 (MIP
1) binding to its cognate receptor CCR5 resulted in activation of
the related adhesion focal tyrosine kinase (RAFTK), with subsequent
activation of the cytoskeletal protein paxillin and the downstream
transcriptional activators, c-Jun N-terminal kinase
(JNK)/stress-activated protein kinase (SAPK) and p38 mitogen-activated protein (MAP) kinase. Inhibition of RAFTK by a dominant-negative kinase
mutant markedly attenuated JNK/SAPK activity. Thus, RAFTK appears to
provide a functional "bridge" for the transmission of CCR5
receptor signaling to the cytoskeleton and nucleus, primary sites of
chemotaxis and growth regulation.
Blood, Vol. 91 No. 3 (February 1), 1998:
pp. 791-797
© 1998 by The American Society of Hematology.
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