Actin-bundling proteins

Otto, Joann J.

doi:10.1016/0955-0674(94)90123-6

Cited by 112 publications

(72 citation statements)

References 38 publications

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“…Another well characterized actin cross-linking protein is fimbrin, a monomeric protein with two tandem ␣-actinintype actin-binding motifs but no spectrin-like repeats; most fimbrins also have two EF-hand motifs at their NH 2 termini (reviewed by Matsudaira, 1994a;Otto, 1994;Ayscough, 1998;Correia and Matsudaira, 1999). Fimbrins have been identified in budding yeast, ciliates, slime molds, plants, and a variety of animals.…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…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).…”

mentioning

confidence: 99%

“…Similarly, in Dictyostelium, inactivation of a Ca 2ϩ -sensitive ␣-actinin confers only subtle defects (Schleicher et al, 1988;Rivero et al, 1999), although the phenotypic effects are somewhat more pronounced (but still nonlethal) in double mutants defective both in this ␣-actinin and in a second actin cross-linking protein (either ABP-120 or the 34-kDa actin-bundling protein) (Rivero et al, 1996(Rivero et al, , 1999. Taken together, the available data suggest that ␣-actinin might be redundant or overlapping in function with other proteins, but the identities of the redundant proteins and the degree of redundancy remain unclear.Another well characterized actin cross-linking protein is fimbrin, a monomeric protein with two tandem ␣-actinintype actin-binding motifs but no spectrin-like repeats; most fimbrins also have two EF-hand motifs at their NH 2 termini (reviewed by Matsudaira, 1994a;Otto, 1994;Ayscough, 1998;Correia and Matsudaira, 1999). Fimbrins have been identified in budding yeast, ciliates, slime molds, plants, and a variety of animals.…”

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confidence: 99%

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

Bähler

Pringle

2001

MBoC

144

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: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

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

Bähler

Pringle

2001

MBoC

144

183

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“…Fascin is an actin-bundling protein that induces cell membrane protrusions and increases motility of normal and transformed epithelial cells (Otto, 1994;Edwards et al, 1995). Fascin protein distributes in structures containing actin bundles including filopodia and stress fibers, causing F-actin to aggregate side-byside into bundles (Yamashiro-Matsumura et al, 1986).…”

Section: Introductionmentioning

confidence: 99%

Comprehensive Bioinformation Analysis of the MRNA Profile of Fascin Knockdown in Esophageal Squamous Cell Carcinoma

Wu¹,

Luo²,

Li³

et al. 2013

Asian Pacific Journal of Cancer Prevention

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Background: Fascin, an actin-bundling protein forming actin bundles including filopodia and stress fibers, is overexpressed in multiple human epithelial cancers including esophageal squamous cell carcinoma (ESCC). Previously we conducted a microarray experiment to analyze fascin knockdown by RNAi in ESCC. Method: In this study, the differentially expressed genes from mRNA expression profilomg of fascin knockdown were analyzed by multiple bioinformatics methods for a comprehensive understanding of the role of fascin. Results: Gene Ontology enrichment found terms associated with cytoskeleton organization, including cell adhesion, actin filament binding and actin cytoskeleton, which might be related to fascin function. Except GO categories, the differentially expressed genes were annotated by 45 functional categories from the Functional Annotation Chart of DAVID. Subpathway analysis showed thirty-nine pathways were disturbed by the differentially expressed genes, providing more detailed information than traditional pathway enrichment analysis. Two subpathways derivated from regulation of the actin cytoskeleton were shown. Promoter analysis results indicated distinguishing sequence patterns and transcription factors in response to the co-expression of downregulated or upregulated differentially expressed genes. MNB1A, c-ETS, GATA2 and Prrx2 potentially regulate the transcription of the downregulated gene set, while Arnt-Ahr, ZNF42, Ubx and TCF11-MafG might co-regulate the upregulated genes. Conclusions: This multiple bioinformatic analysis helps provide a comprehensive understanding of the roles of fascin after its knockdown in ESCC.

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Actin‐Binding Proteins

Lindberg

Schutt²

2002

Encyclopedia of Molecular Biology

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Actin-bundling proteins

Cited by 112 publications

References 38 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

Comprehensive Bioinformation Analysis of the MRNA Profile of Fascin Knockdown in Esophageal Squamous Cell Carcinoma

Actin‐Binding Proteins

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