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
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DOI:
10.1016/j.bbrc.2007.05.162
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发表时间:
2007-08-10
影响因子:
3.1
通讯作者:
Pohajdak, Bill
中科院分区:
文献类型:
--
作者:
MacNeil, Adam J.;Mansour, Marc;Pohajdak, Bill
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. (c) 2007 Elsevier Inc. All rights reserved.