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Ko, J. et al.

Ko, Jang, Kim, Kim, Sung, Kim, Park, Lee, Kim, Na,

Human LZIP binds to CCR1 and differentially affects the chemotactic activities of CCR1-dependent chemokines.

Signaling molecules that bind to chemokine receptors should play key roles in regulation of cell migration induced by chemokines. To characterize the CCR1-mediated cellular signal transduction mechanism, we used the yeast two-hybrid system to identify a cellular ligand for CCR1. LZIP, which has been known as a transcription factor in various cell types, was identified as a CCR1 binding protein. Although the ability of LZIP to bind DNA is possibly what allows it to function as a transcription factor, its detailed function and participation in chemotaxis have not been established. We found that LZIP binds to CCR1 based on results of a mammalian two-hybrid assay and immunoprecipitation experiments. The 21-260 residues of LZIP were essential for interaction with CCR1. Results from a chemotaxis assay using LZIP transfected cells showed that LZIP enhanced Lkn-1-induced chemotaxis, whereas the chemotactic activities induced by other CC chemokines that bind to CCR1, including MIP-1alpha, RANTES, or HCC-4, were not affected by LZIP overexpression. These data indicate that LZIP binds to CCR1 and that the interaction between CCR1 and LZIP participates in regulation of Lkn-1-dependent cell migration without affecting the chemotactic activities of other CC chemokines that bind to CCR1.[1]

References

Human LZIP binds to CCR1 and differentially affects the chemotactic activities of CCR1-dependent chemokines. Ko, J., Jang, S.W., Kim, Y.S., Kim, I.S., Sung, H.J., Kim, H.H., Park, J.Y., Lee, Y.H., Kim, J., Na, D.S. FASEB J. (2004) [Pubmed]

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