Identification of a Phosphatidylinositol 4,5-Bisphosphate-binding Site in Chicken Skeletal Muscle α-Actinin

Fukami, Kiyoko; Sawada, Norio; Endo, Takeshi; Takenawa, Tadaomi

doi:10.1074/jbc.271.5.2646

Cited by 111 publications

(104 citation statements)

References 40 publications

(38 reference statements)

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“…Ain1p and the Drosophila protein are also ϳ30% identical over their COOH-terminal ϳ70 amino acids. No other obvious motifs were found in Ain1p, except for one small region (amino acids 137-153) having 47% identity (65% similarity) to the phosphatidylinositol 4,5-bisphosphate-binding site in chicken muscle ␣-actinin (Fukami et al, 1996).…”

Section: Identification Of An ␣-Actinin Homologue and Of A Fimbrin Inmentioning

confidence: 99%

“…Both proteins have regions with recognizable similarity to EF hands, but none of these regions seems likely to be functional for Ca 2ϩ binding (Strynadka and James, 1989), so that neither Ain1p nor Fim1p seems likely to be regulated by Ca 2ϩ . ␣-Actinins have been found to bind phosphatidylinositol 4,5-bisphosphate and to interact with several proteins, including CRP1, integrin, vinculin, and zyxin (Fukami et al, 1996;Pomiès et al, 1997; and references cited therein). Ain1p has one possible phosphatidylinositol 4,5-bisphosphate binding site, and a CRP1 homologue (accession number Q14014) has been identified by the genome project, so that these elements may be important in the regulation of Ain1p.…”

Section: Possible Regulation Of Ain1p and Fim1pmentioning

confidence: 99%

See 1 more Smart Citation

Roles of a Fimbrin and an α-Actinin-like Protein in Fission Yeast Cell Polarization and Cytokinesis

Bähler

Pringle

2001

MBoC

143

183

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Eukaryotic cells contain many actin-interacting proteins, including the ␣-actinins and the fimbrins, both of which have actin cross-linking activity in vitro. We report here the identification and characterization of both an ␣-actinin-like protein (Ain1p) and a fimbrin (Fim1p) in the fission yeast Schizosaccharomyces pombe. Ain1p localizes to the actomyosin-containing medial ring in an F-actindependent manner, and the Ain1p ring contracts during cytokinesis. ain1 deletion cells have no obvious defects under normal growth conditions but display severe cytokinesis defects, associated with defects in medial-ring and septum formation, under certain stress conditions. Overexpression of Ain1p also causes cytokinesis defects, and the ain1 deletion shows synthetic effects with other mutations known to affect medial-ring positioning and/or organization. Fim1p localizes both to the cortical actin patches and to the medial ring in an F-actin-dependent manner, and several lines of evidence suggest that Fim1p is involved in polarization of the actin cytoskeleton. Although a fim1 deletion strain has no detectable defect in cytokinesis, overexpression of Fim1p causes a lethal cytokinesis defect associated with a failure to form the medial ring and concentrate actin patches at the cell middle. Moreover, an ain1 fim1 double mutant has a synthetical-lethal defect in medial-ring assembly and cell division. Thus, Ain1p and Fim1p appear to have an overlapping and essential function in fission yeast cytokinesis. In addition, protein-localization and mutant-phenotype data suggest that Fim1p, but not Ain1p, plays important roles in mating and in spore formation. INTRODUCTIONThe actin cytoskeleton is involved in many processes in eukaryotic cells, including the polarization of cell growth and cytokinesis. These many roles involve the interaction of actin with a wide variety of actin-binding proteins, including proteins that can cross-link actin filaments into isotropic gels or bundles. Many actin cross-linking proteins have been purified and studied in vitro, but their functions in vivo remain poorly understood (reviewed by Matsudaira, 1994a;Otto, 1994;Furukawa and Fechheimer, 1997;Ayscough, 1998;Bartles, 2000).Among the actin cross-linking proteins, one of the best characterized is ␣-actinin. It was first isolated from rabbit skeletal muscle (Ebashi and Ebashi, 1965) and has subsequently been identified in both muscle and nonmuscle cells from a variety of animals, in Acanthamoeba, and in Dictyostelium (Furukawa and Fechheimer, 1997;Critchley and Flood, 1999). ␣-Actinin forms a homodimer of antiparallel polypeptides (Critchley and Flood, 1999;Djinovic-Carugo et al., 1999), with the actin-binding domain of each polypeptide close to the NH 2 terminus, followed by four spectrin-like repeats and two COOH-terminal EF-hand motifs. Skeletal muscle isoforms are localized to the Z-disk and are not regulated by Ca 2ϩ , whereas nonmuscle isoforms are localized to focal adhesions, stress fibers, and other structures and are typically regulated by C...

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Section: Identification Of An ␣-Actinin Homologue and Of A Fimbrin Inmentioning

confidence: 99%

Section: Possible Regulation Of Ain1p and Fim1pmentioning

confidence: 99%

Roles of a Fimbrin and an α-Actinin-like Protein in Fission Yeast Cell Polarization and Cytokinesis

Bähler

Pringle

2001

MBoC

143

183

View full text Add to dashboard Cite

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“…Calcium binding to the EF hand modules in ␣-actinin decreases the interaction between ␣-actinin and actin (26,27). Fukami et al (28,29) have shown that the skeletal muscle isoform of ␣-actinin binds phosphatidylinositol 4,5-bisphosphate and that the actin gelating activity of the protein was enhanced by the phospholipid. More recently, Greenwood et al (30) reported that in rat embryonic fibroblasts, phosphatidylinositol 3,4,5-triphosphate, a lipid product of phosphatidylinositol 3-kinase, bound to ␣-actinin.…”

mentioning

confidence: 99%

The Cytoskeletal/Non-muscle Isoform of α-Actinin Is Phosphorylated on Its Actin-binding Domain by the Focal Adhesion Kinase

Izaguirre¹,

Aguirre²,

Hu³

et al. 2001

Journal of Biological Chemistry

133

153

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␣-Actinin is tyrosine-phosphorylated in activated human platelets (Izaguirre, G., Aguirre, L., Ji, P., Aneskievich, B., and Haimovich, B. (1999) J. Biol. Chem. 274, 37012-37020). Analysis of platelet RNA by reverse transcription-polymerase chain reaction revealed that ␣-actinin expressed in platelets is identical to the cytoskeletal/non-muscle isoform. A construct of this isoform containing a His 6 tag at the amino terminus was generated. Robust tyrosine phosphorylation of the recombinant protein was detected in cells treated with the tyrosine phosphatase inhibitor vanadate. The tyrosine phosphorylation site was localized to the amino-terminal domain by proteolytic digestion. A recombinant ␣-actinin protein containing a Tyr 3 Phe mutation at position 12 (Y12F) was no longer phosphorylated when expressed in vanadate-treated cells, indicating that tyrosine 12 is the site of phosphorylation. The wild type recombinant protein was not phosphorylated in cells lacking the focal adhesion kinase (FAK). Re-expression of FAK in these cells restored ␣-actinin phosphorylation. Purified wild type ␣-actinin, but not the Y12F mutant, was phosphorylated in vitro by wild type as well as a Phe-397 mutant of FAK. In contrast, no phosphorylation was detected in the presence of a kinase-dead FAK. Tyrosine phosphorylation reduced the amount of ␣-actinin that cosedimented with actin filaments. These results establish that ␣-actinin is a direct substrate for FAK and suggest that ␣-actinin mediates FAK-dependent signals that could impact the physical properties of the cytoskeleton.

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“…PIP 2 1 modulates many actin regulatory proteins in vitro and includes the following: actin severing and/or capping proteins (6 -8); monomer-binding proteins (9 -11); the actin-nucleating protein, N-WASP/Arp2/3 (12); and actin cross-linking proteins (13,14). It has been hypothesized that PIP 2 induces actin assembly by dissociating capping proteins from filament ends, releasing actin monomers from actin-sequestering proteins, inhibiting actin severing, stimulating actin nucleation, and increasing or decreasing actin cross-linking (1,13,(15)(16)(17). In general, PIP 2 predisposes the actin cytoskeleton to a "polymerization mode" and assists its remodeling as well as its interaction with the plasma membrane.…”

mentioning

confidence: 99%

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

Kumar

Zhao

Tomar

et al. 2004

Journal of Biological Chemistry

100

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Identification of a Phosphatidylinositol 4,5-Bisphosphate-binding Site in Chicken Skeletal Muscle α-Actinin

Cited by 111 publications

References 40 publications

Roles of a Fimbrin and an α-Actinin-like Protein in Fission Yeast Cell Polarization and Cytokinesis

Roles of a Fimbrin and an α-Actinin-like Protein in Fission Yeast Cell Polarization and Cytokinesis

The Cytoskeletal/Non-muscle Isoform of α-Actinin Is Phosphorylated on Its Actin-binding Domain by the Focal Adhesion Kinase

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

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