Dephosphorylation of cofilin in stimulated platelets: roles for a GTP-binding protein and Ca2+.
Explore this paper's citation graph
Summary
Cofilin is added to the actin-binding proteins that may regulate the platelet cytoskeleton, and suggest that platelet cofilin can be activated by dephosphorylation reactions initiated either by a GTP-binding protein or Ca2+.
- Type
- article
- Published
- 1994-07-01
- Cited by
- 81
- References
- 3
- Access
- Open access
- OpenAlex
- https://openalex.org/W1518379473
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:19792925
Keywords
Dephosphorylation, Cofilin, Phosphorylation, Biochemistry, Myosin light-chain kinase
References
Cited by
- Actin-Binding Proteins in Plant Cells
- Analysis of GTP-binding proteins, phosphoproteins, and cytosolic calcium in functional heterogeneous human blood platelet subpopulations.
- CASEIN KINASE1-LIKE PROTEIN2 Regulates Actin Filament Stability and Stomatal Closure via Phosphorylation of Actin Depolymerizing Factor
- Actin dynamics in platelets.
- Functional analysis of the LIM kinase 1 and its role in cell cycle progression
- Normal Arp2/3 complex activation in platelets lacking WASp.
- Dephosphorylation of Serine 3 Regulates Nuclear Translocation of Cofilin*
- Signaling pathways regulating LIM-kinase-1 activation and cofilin phosphorylation in activated platelets
- Regulation of LIM-kinase 1 and cofilin in thrombin-stimulated platelets.
- Rac, a small guanosine triphosphate-binding protein, and p21-activated kinase are activated during platelet spreading on collagen-coated surfaces: roles of integrin alpha(2)beta(1).
- Platelet‐Fibrinogen Interactions
- Protein Tyrosine Kinases and Protein Tyrosine Phosphatases Are Involved in Abscisic Acid-Dependent Processes in Arabidopsis Seeds and Suspension Cells1
- Phosphorylation of Ser‐3 of cofilin regulates its essential function on actin
- Upregulation of profilin, cofilin-2 and LIMK2 in cultured pulmonary artery smooth muscle cells and in pulmonary arteries of monocrotaline-treated rats.
- Molecular mechanism of cofilin dephosphorylation by ouabain.
- Concentration of cofilin, a small actin-binding protein, at the cleavage furrow during cytokinesis.
- Towards Scarless Wound Healing: A Comparison of Protein Expression between Human, Adult and Foetal Fibroblasts
- Site-directed mutagenesis of the phosphorylation site of cofilin: its role in cofilin-actin interaction and cytoplasmic localization.
- Identification of Two 17-kDa Rat Parotid Gland Phosphoproteins, Subjects for Dephosphorylation upon β-Adrenergic Stimulation, as Destrin- and Cofilin-like Proteins (*)
- Reactivation of Phosphorylated Actin Depolymerizing Factor and Identification of the Regulatory Site (*)
Related papers
- Involvement of Slingshot in the Rho-mediated Dephosphorylation of ADF/Cofilin during Xenopus Cleavage
- Dephosphorylation of cofilin in polymorphonuclear leukocytes derived from peripheral blood.
- Reestablishment of Hepatocytic Polarity in Vitro and Dephosphorylation of Cofilin
- Investigation of mechanism of apoptosis via inhibiting myosin light chain kinase
- Dephosphorylation of clustered phosphoserine residues in human Grb14 by protein phosphatase 1 and its effect on insulin receptor complex formation
- Signaling pathways involved in dephosphorylation and localization of the actin-binding protein cofilin in stimulated human neutrophils.
- Inhibition of membrane phosphotyrosyl-protein phosphatase activity by vanadate.
- Structure-function relationships in smooth muscle myosin light chain kinase.
- DTL-DephosSite: Deep Transfer Learning Based Approach to Predict Dephosphorylation Sites