Baig, Akeel; Bao, Xiankun; Wolf, Marlene; Haslam, Richard J (2009). The platelet protein kinase C substrate pleckstrin binds directly to SDPR protein. Platelets, 20(7), pp. 446-457. London: Informa Healthcare 10.3109/09537100903137314
Full text not available from this repository.Pleckstrin is a modular platelet protein consisting of N- and C-terminal pleckstrin homology (PH) domains, a central dishevelled egl10 and pleckstrin (DEP) domain and a phosphorylation region. Following agonist-induced platelet stimulation, dimeric pleckstrin translocates to the plasma membrane, is phosphorylated and then monomerizes. A recent study found that pleckstrin null platelets from a knockout mouse have a defect in granule secretion, actin polymerization and aggregation. However, the mechanism of pleckstrin signaling for this function is unknown. Our recent studies have led to the identification of a novel pleckstrin-binding protein, serum deprivation response protein (SDPR), by co-immunoprecipitation, GST-pulldowns and nanospray quadruple time of flight mass spectrometry. We show that this interaction occurs directly through N-terminal sequences of pleckstrin. Both pleckstrin and SDPR are phosphorylated by protein kinase C (PKC), but the interaction between pleckstrin and SDPR was shown to be independent of PKC inhibition or activation. These results suggest that SDPR may facilitate the translocation of nonphosphorylated pleckstrin to the plasma membrane in conjunction with phosphoinositides that bind to the C-terminal PH domain. After binding of pleckstrin to the plasma membrane, its phosphorylation by PKC exerts downstream effects on platelet aggregation/secretion.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
04 Faculty of Medicine > Pre-clinic Human Medicine > Theodor Kocher Institute |
UniBE Contributor: |
Wolf, Marlene |
ISSN: |
0953-7104 |
Publisher: |
Informa Healthcare |
Language: |
English |
Submitter: |
Factscience Import |
Date Deposited: |
04 Oct 2013 15:13 |
Last Modified: |
05 Dec 2022 14:22 |
Publisher DOI: |
10.3109/09537100903137314 |
PubMed ID: |
19852682 |
Web of Science ID: |
000272718400001 |
URI: |
https://boris.unibe.ch/id/eprint/32148 (FactScience: 197075) |
Actions (login required)
 |
Edit item |