Abstract:
:Granulocyte colony-stimulating factor (G-CSF) is the major cytokine involved in the control of neutrophil development. G-CSF activates the special receptor, the G-CSF receptor (GCSF-R), which subsequently triggers multiple signaling events. To obtain more interactive molecules with GCSF-R and to further understand the cellular signaling mechanism of GCSF-R, yeast two-hybrid system was used to screen a mouse liver library. Here, the interaction of GCSF-R and Snapin was found by yeast two-hybrid experiment, and the interaction of the two proteins was further confirmed by GST pull-down experiment, mammalian two-hybrid experiment and co-immunoprecipitation study. Moreover, the immuno-fluorescence assay was shown that the two proteins of GCSF-R with Snapin were co-localized in the cytoplasm and plasma membrane. The region of C-terminal GCSF-R between box2 and box3, including the residue Tyr703, was responsible for the interaction with Snapin. These data suggested that Snapin is a new interactive protein of GCSF-R.
journal_name
Cytokinejournal_title
Cytokineauthors
Yuan X,Shan Y,Zhao Z,Chen J,Cong Ydoi
10.1016/j.cyto.2006.01.008subject
Has Abstractpub_date
2006-02-21 00:00:00pages
219-25issue
4eissn
1043-4666issn
1096-0023pii
S1043-4666(06)00048-2journal_volume
33pub_type
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