Molecular cloning of a novel actin‐binding protein, p57, with a WD repeat and a leucine zipper motif

Suzuki, Kensuke; Nishihata, Jun; Arai, Yūkō; Honma, Nakayuki; Yamamoto, Kazuo; Irimura, Tatsuro; Toyoshima, Satoshi

doi:10.1016/0014-5793(95)00393-n

Cited by 100 publications

(102 citation statements)

References 19 publications

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“…The level of the ClipinC mRNA was extremely high in the brain, moderate in heart and ovary, and very low or undetectable in the other tissues examined in this study. As previously reported (12), the ClipinA transcript was mainly detected only in immune system tissues, i.e. spleen, thymus, and peripheral leukocytes.…”

Section: Resultssupporting

confidence: 84%

“…Analysis of the FC96 protein sequence with a protein data base disclosed an overall similarity to the Dictyostelium coronin (38.5%) and its mammalian homologs, i.e. p57 (43.9%) (12) and IR10 (61.0%) (13). An amino-terminal domain containing five WD repeats and a succeeding domain covering about 100 amino acids with a tendency to form an ␣-helical structure were well conserved among these molecules.…”

Section: Resultsmentioning

confidence: 99%

“…Northern Blot Analysis-Human multiple tissue blots I and II (CLONTECH) were hybridized as described before (11) with DNA probes: ClipinA/p57 (nucleotides 489 -930) (12), ClipinB/IR10 (nucleotides 372-1333) (13), and ClipinC (nucleotides 587-1602). The ClipinA and B probes used were the reverse transcription-polymerase chain reaction products from human brain poly(A) ϩ RNA (CLONTECH).…”

Section: Methodsmentioning

confidence: 99%

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A Neurally Enriched Coronin-like Protein, ClipinC, Is a Novel Candidate for an Actin Cytoskeleton-Cortical Membrane-linking Protein

Nakamura¹,

Takeuchi²,

Muraoka³

et al. 1999

Journal of Biological Chemistry

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Brain-enriched human FC96 protein shows a close sequence similarity to the Dictyostelium actin-binding protein coronin, which has been implicated in cell motility, cytokinesis, and phagocytosis. A phylogenetic tree analysis revealed that FC96 and two other mammalian molecules (p57 and IR10) form a new protein family, the coronin-like protein (Clipin) family; thus hereafter we refer to FC96 as ClipinC. A WD domain and a succeeding ␣-helical region are conserved among coronin and Clipin family members. ClipinC is predominantly expressed in the brain, and discrete areas in the mouse brain were intensely labeled with anti-ClipinC antibodies. ClipinC was also shown to bind directly to F-actin in vitro. Immunocytochemical analysis revealed that ClipinC accumulated at focal adhesions as well as at neurite tips and stress fibers. Furthermore, ClipinC was associated with vinculin, which is a major component of focal contacts. These results indicate that ClipinC is also a component part of the cross-bridge between the actin cytoskeleton and the plasma membrane. These findings and the previously reported function of coronin suggest that ClipinC may play specific roles in the reorganization of neuronal actin structure, a change that has been implicated in both cell motility and growth cone advance.Actin filaments in neuronal cells form a cortical framework that helps to localize membrane proteins, and F-actin dynamics has been implicated in directing neuronal outgrowth. Rearrangement of the actin cytoskeleton occurs in response to various stimuli such as soluble factors or attachment to a substratum (1, 2). The regulation of F-actin patterns involves actin polymerization and actin cross-linking. Factors regulating these processes communicate with the small G proteins of the Rho family (3) and the phosphatidylinositol metabolism system (4), both of which are triggered by extracellular cues through a variety of receptors.The Dictyostelium actin-binding protein coronin was first purified from an actin-myosin complex and was hypothesized to transmit signals from the membrane receptors to the cortical cytoskeleton (5). Coronin accumulates at the leading edges of moving cells and in crown-shaped extensions on the dorsal cell surface. The involvement of coronin in cell motility, cytokinesis, and phagocytosis, all of which depend on cytoskeletal rearrangement, has been demonstrated by use of a gene replacement mutant. In a mutant that lacks coronin, cell motility is reduced to less than half of the normal speed, and cytoplasmic cleavage in cytokinesis is impaired (6). Further, in the coronin null (cor Ϫ ) mutant, the rate of yeast uptake is reduced by about 70% (7). However, the distribution of actin filaments in cor Ϫ cells is similar to that in the wild-type ones (6).In this study, we found a novel candidate for an actin cytoskeleton-cortical membrane linking protein; this protein, ClipinC, is also the third member of a family of mammalian homologs of Dictyostelium coronin. The ClipinC transcript was predominantly expressed in th...

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Section: Resultssupporting

confidence: 84%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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A Neurally Enriched Coronin-like Protein, ClipinC, Is a Novel Candidate for an Actin Cytoskeleton-Cortical Membrane-linking Protein

Nakamura¹,

Takeuchi²,

Muraoka³

et al. 1999

Journal of Biological Chemistry

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“…Detailed description was made in this study for three zebrafish homologues, coro1a, nephrosin, and dab2, that exhibited specific expression in hematopoietic͞ vascular tissues, but whose functions in mammals are poorly understood. Although there is currently no functional data on human CORO1A, mouse Coro1A has been shown to contain a WD (trp͞asp) repeat and a leucine zipper motif (26) and to reside on phagosomal membranes in cells infected by mycobacteria, thus preventing endocytic transport of these bacteria to lysosomes and promoting their intracellular survival in cultured macrophages (27). This observation is consistent with our results that coro1a is expressed in myeloid cells coexpressing mpo and indicates that coro1a is a marker for mature granulocyte and monocytes.…”

Section: Discussionmentioning

confidence: 99%

Hematopoietic gene expression profile in zebrafish kidney marrow

Song

Sun

Deng

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

141

101

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The zebrafish kidney marrow is considered to be the organ of definitive hematopoiesis, analogous to the mammalian bone marrow. We have sequenced 26,143 ESTs and isolated 304 cDNAs with putative full-length ORF from a zebrafish kidney marrow cDNA library. The ESTs formed 7,742 assemblies, representing both previously identified zebrafish ESTs (56%) and recently discovered zebrafish ESTs (44%). About 30% of these EST assemblies have orthologues in humans, including 1,282 disease-associated genes in the Online Mendelian Inheritance in Man (OMIM) database. Comparison of the effective and regulatory molecules related to erythroid functions across species suggests a good conservation from zebrafish to human. Interestingly, both embryonic and adult zebrafish globin genes showed higher homology to the human embryonic globin genes than to the human fetal͞adult ones, consistent with evo-devo correlation hypothesis. In addition, conservation of a whole set of transcription factors involved in globin gene switch suggests the regulatory network for such remodeling mechanism existed before the divergence of the teleost and the ancestor of mammals. We also carried out whole-mount mRNA in situ hybridization assays for 493 cDNAs and identified 80 genes (16%) with tissue-specific expression during the first five days of zebrafish development. Twenty-six of these genes were specifically expressed in hematopoietic or vascular tissues, including three previously unidentified zebrafish genes: coro1a, nephrosin, and dab2. Our results indicate that conserved genetic programs regulate vertebrate hematopoiesis and vasculogenesis, and support the role of the zebrafish as an important animal model for studying both normal development and the molecular pathogenesis of human blood diseases.

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“…All seven proteins are characterized by the presence of evolutionally conserved structural domains that include tryptophan/aspartic acid repeats that are implicated in the association with actin filaments. We previously identified p57/coronin-1 as the first mammalian coronin and found that this protein was selectively expressed in immune cells (9). We have also reported that p57/coronin-1 possesses at least two actin binding regions (10) and forms a homodimer via a leucine zipper motif present in the C-terminal coiled-coil region (11).…”

mentioning

confidence: 99%

Constitutive Turnover of Phosphorylation at Thr-412 of Human p57/Coronin-1 Regulates the Interaction with Actin

Oku

Nakano

Kaneko

et al. 2012

Journal of Biological Chemistry

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Background: Biological functions of actin-binding protein p57/coronin-1 may be regulated by phosphorylation. Results: Ser-2 and Thr-412 were identified as major phosphorylation sites of p57/coronin-1, and the phosphorylation at Thr-412 reduced the binding affinity for actin. Conclusion: Physical interaction between p57/coronin-1 and actin is regulated by phosphorylation at Thr-412. Significance: The results provide mechanistic insight into the actin-related immunological processes.

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Molecular cloning of a novel actin‐binding protein, p57, with a WD repeat and a leucine zipper motif

Cited by 100 publications

References 19 publications

A Neurally Enriched Coronin-like Protein, ClipinC, Is a Novel Candidate for an Actin Cytoskeleton-Cortical Membrane-linking Protein

A Neurally Enriched Coronin-like Protein, ClipinC, Is a Novel Candidate for an Actin Cytoskeleton-Cortical Membrane-linking Protein

Hematopoietic gene expression profile in zebrafish kidney marrow

Constitutive Turnover of Phosphorylation at Thr-412 of Human p57/Coronin-1 Regulates the Interaction with Actin

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