Title: Roles of Src-like adaptor protein 2 (SLAP-2) in GPVI-mediated platelet activation SLAP-2 and GPVI signaling
Authors: Sugihara, Sayaka ×
Katsutani, Shinya
Deckmyn, Hans
Fujimura, Kingo
Kimura, Akiro #
Issue Date: Oct-2010
Publisher: Pergamon Press
Series Title: Thrombosis Research vol:126 issue:4 pages:E276-E285
Abstract: BACKGROUND: Glycoprotein VI (GPVI) /Fc receptor gamma (FcRγ)-chain complex is one of the collagen receptors in platelets and responsible for the majority of the intracellular signaling events through a similar pathway to immune receptors. Src-like adaptor protein 2 (SLAP-2) is a recently characterized adaptor protein predominantly expressed in hematopoietic cells. In T cells, SLAP-2 was reported to associate with several tyrosine phosphorylated proteins, and function as a negative regulator of signaling downstream of T cell antigen receptor by virtue of its interaction with the ubiquitin ligase c-Cbl. But the data regarding the presence and role of SLAP-2 proteins in platelets is limited. OBJECTIVES: We describe the characterization of SLAP-2 in human platelets. METHODS: Human platelets were analyzed by Western blot analysis, immunoprecipitation, and pull down assay, etc. RESULTS: Immunoprecipitation revealed the presence of two forms of SLAP-2 with approximately 28kD and 25kD, and following stimulation of GPVI, the additional form with approximately 32kD apppeared. We have found that upon GPVI activation, SLAP-2 translocated from the Triton X-100-soluble fraction to the Triton X-100-insoluble cytoskeleton fraction, with concomitant association with Syk, c-Cbl, and LAT. CONCLUSIONS: SLAP-2 appears to play a role in regulating signaling pathways by bringing important signaling molecules such as c-Cbl and Syk into proximity of cytoskeletal substrates. In platelets, SLAP-2 may have function as a negative regulator of GPVI-mediated signaling by interacting with c-Cbl, being similar to that reported in T cells.
ISSN: 0049-3848
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Interdisciplinary Research Facility Life Sciences, Campus Kulak Kortrijk
Chemistry, Campus Kulak Kortrijk
× corresponding author
# (joint) last author

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