کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1937526 | 1050719 | 2007 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Sorting nexin 27 interacts with the Cytohesin associated scaffolding protein (CASP) in lymphocytes Sorting nexin 27 interacts with the Cytohesin associated scaffolding protein (CASP) in lymphocytes](/preview/png/1937526.png)
CASP is a small cytokine-inducible protein, primarily expressed in hematopoetic cells, which associates with members of the Cytohesin/ARNO family of guanine nucleotide-exchange factors. Cytohesins activate ARFs, a group of GTPases involved in vesicular initiation. Functionally, CASP is an adaptor protein containing a PDZ domain, a coiled-coil, and a potential carboxy terminal PDZ-binding motif that we sought to characterize here. Using GST pulldowns and mass spectrometry we identified the novel interaction of CASP and sorting nexin 27 (SNX27). In lymphocytes, CASP’s PDZ-binding motif interacts with the PDZ domain of SNX27. This protein is a unique member of the sorting nexin family of proteins, a group generally involved in the endocytic and intracellular sorting machinery. Endogenous SNX27 and CASP co-localize at the early endosomal compartment in lymphocytes and also in transfection studies. These results suggest that endosomal SNX27 may recruit CASP to orchestrate intracellular trafficking and/or signaling complexes.
Journal: Biochemical and Biophysical Research Communications - Volume 359, Issue 4, 10 August 2007, Pages 848–853