Inositol phospholipid — Induced suppression of F-actin-gelating activity of smooth muscle filamin

Furuhashi, Kiyoshi; Inagaki, Masaki; Hatano, Sadashi; Fukami, Kiyoko; Takenawa, Tadaomi

doi:10.1016/s0006-291x(05)80018-x

Cited by 52 publications

(27 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In our overlay assay, the F-actin binding site does not contribute to the binding of PKC, although these CH domains bind to and insert in phospholipid bilayers (30,51). Furthermore, acidic phospholipids inhibit F-actin cross-linking by filamin (33). This indicates that lipid binding of filamin is re- quired but not sufficient to support an interaction with PKC␣ and protein-protein binding contributes to their interaction.…”

Section: Discussionmentioning

confidence: 76%

“…Binding to phospholipids (30), phosphorylation by serine/threonine kinases (31), and proteolytic cleavage (32) seem involved. Evidence from in vitro assays indicates that phospholipids inhibit actin organization by turkey gizzard filamin (33) and phosphorylation by Ca 2ϩ / calmodulin-dependent kinase II decreases its actin binding affinity (34). Resistance of FLNa to calpain cleavage is increased after phosphorylation of FLNa through protein kinase A (PKA) (32).…”

mentioning

confidence: 99%

See 1 more Smart Citation

The F-actin Cross-linking and Focal Adhesion Protein Filamin A Is a Ligand and in Vivo Substrate for Protein Kinase Cα

Tigges

Koch

Wissing

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

Filamin A is an established structural component of cell-matrix adhesion sites. In addition, it serves as a scaffold for the subcellular targeting of different signaling molecules. Protein kinase C (PKC) has been found associated with filamin; however, details about this interaction and its significance for cell-matrix adhesiondependent signaling have remained elusive. We performed a yeast two-hybrid analysis using protein kinase C␣ as a bait and identified filamin as a direct binding partner. The interaction was confirmed in transfected HeLa cells, and serial truncation fragments of filamin A were employed to identify two binding sites on filamin. In vitro ligand binding assays revealed a Ca 2؉ and phospholipid-dependent association of the regulatory domain of protein kinase C with these sites. Phosphorylation of filamin was found to be isoform-restricted, leading to phosphate incorporation in the C termini of filamin A and C, but not B. PKC-dependent phosphorylation of filamin was also detected in cells. Our data suggest an intimate interaction between filamin and PKC in cell signaling.

show abstract

Section: Discussionmentioning

confidence: 76%

mentioning

confidence: 99%

The F-actin Cross-linking and Focal Adhesion Protein Filamin A Is a Ligand and in Vivo Substrate for Protein Kinase Cα

Tigges

Koch

Wissing

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…In contrast, there is significant association of villin with vesicles containing the phosphoinositides, PI, PIP, or PIP 2 , with the following binding profile: PIP 2 Ͼ PIP Ͼ PI. Similar phosphoinositide-specific binding is also known for other actin-binding proteins of the villin family (4,45). Because villin binds to PIP 2 with the highest affinity, all experiments in this report were done examining the effect of the association of villin with PIP 2 .…”

Section: Characterization Of the Association Of Villin Withmentioning

confidence: 71%

Association of Villin with Phosphatidylinositol 4,5-Bisphosphate Regulates the Actin Cytoskeleton

Kumar

Zhao

Tomar

et al. 2004

Journal of Biological Chemistry

100

View full text Add to dashboard Cite

“…A proteomic analysis of E. histolytica uroids identified the presence of actin-binding proteins that have been reported to interact with PI(4,5)P 2 in other eukaryotic cells, including the spectrin-family proteins (e.g., filamin 2, an actininlike protein) and a novel protein, filopodin (53). In other systems, PI(4,5)P 2 has been shown to regulate actin cytoskeleton by binding and modulating filamin (54) and ␣-actinin (55). Filopodin is an ezrin-radixin-moesin (ERM) domain-containing protein.…”

Section: Discussionmentioning

confidence: 99%

Localization of Phosphatidylinositol 4,5-Bisphosphate to Lipid Rafts and Uroids in the Human Protozoan Parasite Entamoeba histolytica

2013

View full text Add to dashboard Cite

bEntamoeba histolytica is an intestinal protozoan parasite and is the causative agent of amoebiasis. During invasive infection, highly motile amoebae destroy the colonic epithelium, enter the blood circulation, and disseminate to other organs such as liver, causing liver abscess. Motility is a key factor in E. histolytica pathogenesis, and this process relies on a dynamic actomyosin cytoskeleton. In other systems, phosphatidylinositol 4,5-bisphosphate [PI(4,5)P 2 ] is known to regulate a wide variety of cellular functions, including signal transduction, actin remodeling, and cell motility. Little is known about the role of PI(4,5)P 2 in E. histolytica pathogenicity. In this study, we demonstrate that PI(4,5)P 2 is localized to cholesterol-rich microdomains, lipid rafts, and the actin-rich fractions of the E. histolytica membrane. Microscopy revealed that the trailing edge of polarized trophozoites, uroids, are highly enriched in lipid rafts and their constituent lipid, PI(4,5)P 2 . Polarization and enrichment of uroids and rafts with PI(4,5)P 2 were enhanced upon treatment of E. histolytica cells with cholesterol. Exposure to cholesterol also increased intracellular calcium, which is a downstream effector of PI(4,5)P 2 , with a concomitant increase in motility. Together, our data suggest that in E. histolytica, PI(4,5)P 2 may signal from lipid rafts and cholesterol may play a role in triggering PI(4,5)P 2 -mediated signaling to enhance the motility of this pathogen.T he intestinal parasite Entamoeba histolytica is known to cause amoebic dysentery and liver abscess. E. histolytica enters the human host via contaminated food or water as an environmentally stable cyst. Excystation leads to the release of trophozoites in the small intestine, which colonize the bowel lumen. From here, the parasite can enter two non-mutually exclusive routes of infection, noninvasive or invasive disease (reviewed in reference 1). In the noninvasive mode, the trophozoite encysts and exits the host, whereas in the invasive mode, the parasite adheres to and destroys the colonic epithelium and enters the circulatory system. This results in extraintestinal infection, of which amoebic liver abscess (ALA) is the most common manifestation. Motility is a key virulence function that enables this parasite to cause extraintestinal infection (2).Motile amoebae display a polarized morphology with a pseudopod at the leading edge and a uroid (also referred to as a uropod in other eukaryotic cells) at the trailing edge. A key feature of a polarized cell is the differential distribution of proteins and lipids, including cell surface receptors, signaling molecules, and cytoskeletal elements. For example, the pseudopod of E. histolytica is enriched in F actin, myosin IB (3, 4), and signaling molecules like phosphatidylinositol-3,4,5-trisphosphate [PI(3,4,5)P 3 ] (5), while the uroid is enriched in myosin II and signaling molecules, including an important heterotrimeric adhesin, the galactose/N-acetylgalactosamine (Gal/GalNAc) lectin (6), F actin, and var...

show abstract

Inositol phospholipid — Induced suppression of F-actin-gelating activity of smooth muscle filamin

Cited by 52 publications

References 16 publications

The F-actin Cross-linking and Focal Adhesion Protein Filamin A Is a Ligand and in Vivo Substrate for Protein Kinase Cα

The F-actin Cross-linking and Focal Adhesion Protein Filamin A Is a Ligand and in Vivo Substrate for Protein Kinase Cα

Association of Villin with Phosphatidylinositol 4,5-Bisphosphate Regulates the Actin Cytoskeleton

Localization of Phosphatidylinositol 4,5-Bisphosphate to Lipid Rafts and Uroids in the Human Protozoan Parasite Entamoeba histolytica

Contact Info

Product

Resources

About