Calcineurin is associated with the cytoskeleton of cultured neurons and has a role in the acquisition of polarity.

Ferreira, A; Kincaid, R; Kosik, K S

doi:10.1091/mbc.4.12.1225

Cited by 112Axon Guidance and Neuronal SignalingNeurogenesis and neuroplasticity mechanismsSignaling Pathways in Disease

Calcineurin is associated with the cytoskeleton of cultured neurons and has a role in the acquisition of polarity.

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Ferreira, A, Kincaid, R, Kosik, K S·1993·Molecular Biology of the Cell

DOI 10.1091/mbc.4.12.1225PMC PMC275760

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Abstract

Calcineurin is a calmodulin-dependent serine-threonine phosphatase found in many cell types but most abundant in neurons. To determine its localization in developing neurons, dissociated cultures from embryonic day 15 rat cerebellum were analyzed immunocytochemically after treatment with cytoskeletal-disrupting drugs. During the initial outgrowth of neurites, calcineurin is enriched in growth cones where its localization depends upon the integrity of both microtubules and actin filaments. Treatment with cytochalasin shifts calcineurin from the growth cone to the neurite shaft, and with nocadozole calcineurin translocates to the cell body. Therefore calcineurin is well positioned to mediate interactions between cytoskeletal systems during neurite elongation. By 14 d in culture, when the neurons have developed extensive neuronal contacts and synapses are present, calcineurin is predominantly in the neurite shaft. Incubation of cultured cells with Cyclosporin A or a specific peptide, both of which selectively inhibit calcineurin's phosphatase activity, prevented axonal elongation. Because the microtubule-associated protein tau appears to play a key role in asymmetric neurite elongation, we examined modifications in its phosphorylation state resulting from calcineurin inhibition. In contrast to the normal development of cerebellar macroneurons in which reactivity with the phosphorylation-dependent antibody, tau-1, progressively increases, there was a persistent inhibition of tau-1 reactivity in cells exposed to Cyclosporin A. These findings suggest a role for calcineurin in regulating tau phosphorylation and possibly modulating other steps required for the determination of polarity.

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In developing cerebellar and hippocampal neurons, calcineurin is highly concentrated in growth cones, structures that, like spines, contain a dense network of F-actin.
“In developing cerebellar (Ferreira et al., 1993) and hippocampal (Halpain et al., 1997) neurons, calcineurin is highly concentrated in growth cones, structures that, like spines, contain a dense network of F-actin.”
From Regulation of F-Actin Stability in Dendritic Spines by Glutamate Receptors and Calcineurin (1998) · cites this paper as Ferreira et al., 1993
Actin filaments dynamically regulate growth cone motility during axon elongation, and the calcineurin antagonist cyclosporin A inhibits neurite outgrowth in cultured cerebellar neurons.
“Actin filaments dynamically regulate growth cone motility during axon elongation (Forscher et al., 1992), and the calcineurin antagonist cyclosporin A was shown to inhibit neurite outgrowth in cultured cerebellar neurons (Ferreira et al., 1993).”
From Regulation of F-Actin Stability in Dendritic Spines by Glutamate Receptors and Calcineurin (1998) · cites this paper as Ferreira et al., 1993

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Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works
Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
Towbin, H., Staehelin, T., & Gordon, J. (1979) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.76.9.4350 · Cited by 51,421 · see citing works
Short-Term Effects of Nose-Only Cigarette Smoke Exposure on Glutathione Redox Homeostasis, Cytochrome P450 1A1/2 and Respiratory Enzyme Activities in Mice Tissues
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,311 · see citing works
Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116 · see citing works
Assay of proteins in the presence of interfering materials
Bensadoun, A., & Weinstein, D. (1976) · Analytical Biochemistry · doi:10.1016/s0003-2697(76)80064-4 · Cited by 3,191 · see citing works
Growth of a rat neuroblastoma cell line in serum-free supplemented medium.
Bottenstein, J. E., & SATO, G. H. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.1.514 · Cited by 2,282 · see citing works
The establishment of polarity by hippocampal neurons in culture.
Dotti, C., Sullivan, C., & Banker, G. (1988) · The Journal of Neuroscience · doi:10.1523/jneurosci.08-04-01454.1988 · Cited by 1,862 · see citing works
Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation
Clipstone, N. A., & Crabtree, G. R. (1992) · Nature · doi:10.1038/357695a0 · Cited by 1,635 · see citing works
Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau.
Drechsel, D. N., Hyman, A. A., Cobb, M. H., & Kirschner, M. W. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.10.1141 · Cited by 971 · see citing works
Phosphorylation affects the ability of tau protein to promote microtubule assembly.
Lindwall, G., & Cole, R. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42989-9 · Cited by 901 · see citing works
Microtubules containing acetylated alpha-tubulin in mammalian cells in culture.
Piperno, G., LeDizet, M., & Chang, X. J. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.2.289 · Cited by 873 · see citing works
Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone.
Forscher, P., & Smith, S. J. (1988) · The Journal of cell biology · doi:10.1083/jcb.107.4.1505 · Cited by 854 · see citing works
FK-506- and CsA-sensitive activation of the interleukin-2 promoter by calcineurin
O’Keefe, S. J., Tamura, J., Kincaid, R. L., Tocci, M. J., & O’Neill, E. A. (1992) · Nature · doi:10.1038/357692a0 · Cited by 841 · see citing works
Self-citation
Calcineurin phosphatase activity in T lymphocytes is inhibited by FK 506 and cyclosporin A.
Fruman, D. A., Klee, C. B., Bierer, B. E., & Burakoff, S. J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.9.3686 · Cited by 823 · see citing works
ULTRASTRUCTURE AND FUNCTION OF GROWTH CONES AND AXONS OF CULTURED NERVE CELLS
Yamada, K. M., Spooner, B. S., & Wessells, N. K. (1971) · The Journal of Cell Biology · doi:10.1083/jcb.49.3.614 · Cited by 767 · see citing works
Calcineurin: a calcium- and calmodulin-binding protein of the nervous system.
Klee, C. B., Crouch, T. H., & Krinks, M. H. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.12.6270 · Cited by 738 · see citing works
Cross-linker system between neurofilaments, microtubules and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method
Hirokawa, N. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.94.1.129 · Cited by 676 · see citing works
Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons
Cáceres, A., & Kosik, K. S. (1990) · Nature · doi:10.1038/343461a0 · Cited by 657 · see citing works
Self-citation
Growth-associated protein, GAP-43, a polypeptide that is induced when neurons extend axons, is a component of growth cones and corresponds to pp46, a major polypeptide of a subcellular fraction enriched in growth cones.
Meiri, K. F., Pfenninger, K. H., & Willard, M. B. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.10.3537 · Cited by 522 · see citing works
Epitopes that span the tau molecule are shared with paired helical filaments
Kosik, K. S., Orecchio, L. D., Binder, L. I., Trojanowski, J. Q., Lee, V. M.-Y., & Lee, G. S. (1988) · Neuron · doi:10.1016/0896-6273(88)90129-8 · Cited by 497 · see citing works
Self-citation
The switch of tau protein to an Alzheimer‐like state includes the phosphorylation of two serine‐proline motifs upstream of the microtubule binding region.
Biernat, J., Mandelkow, E. M., Schröter, C., Lichtenberg‐Kraag, B., Steiner, B., Berling, B., Meyer, H., Mercken, M., Vandermeeren, A., & Goedert, M. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05204.x · Cited by 484 · see citing works
Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin.
Sobue, K., Muramoto, Y., Fujita, M., & Kakiuchi, S. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.9.5652 · Cited by 425 · see citing works
Experimental observations on the development of polarity by hippocampal neurons in culture.
Goslin, K., & Banker, G. A. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.108.4.1507 · Cited by 416 · see citing works
MAP2 and tau segregate into dendritic and axonal domains after the elaboration of morphologically distinct neurites: an immunocytochemical study of cultured rat cerebrum
Kosik, K., & Finch, E. (1987) · The Journal of Neuroscience · doi:10.1523/jneurosci.07-10-03142.1987 · Cited by 368 · see citing works
Self-citation
Microtubule behavior in the growth cones of living neurons during axon elongation.
Tanaka, E. M., & Kirschner, M. W. (1991) · The Journal of Cell Biology · doi:10.1083/jcb.115.2.345 · Cited by 349 · see citing works
Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins
Griffith, L. M. (1978) · The Journal of Cell Biology · doi:10.1083/jcb.78.3.958 · Cited by 348 · see citing works
Regulation of calmodulin binding to P-57. A neurospecific calmodulin binding protein.
Alexander, K. A., Cimler, B. M., Meier, K. E., & Storm, D. R. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45544-5 · Cited by 333 · see citing works
Overexpression of tau in a nonneuronal cell induces long cellular processes.
Knops, J., Kosik, K. S., Lee, G., Pardee, J. D., Cohen-Gould, L., & McConlogue, L. (1991) · The Journal of cell biology · doi:10.1083/jcb.114.4.725 · Cited by 286 · see citing works
Self-citation
Assembly of microtubules at the tip of growing axons
Bamburg, J. R., Bray, D., & Chapman, K. (1986) · Nature · doi:10.1038/321788a0 · Cited by 279 · see citing works
Identification of an autoinhibitory domain in calcineurin.
Hashimoto, Y., Perrino, B. A., & Soderling, T. R. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39919-3 · Cited by 272 · see citing works
p42 map kinase phosphorylation sites in microtubule‐associated protein tau are dephosphorylated by protein phosphatase 2A<sub>1</sub> Implications for Alzheimer's disease
Goedert, M., Cohen, E. S., Jakes, R., & Cohen, P. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81418-l · Cited by 272 · see citing works
Suppression of MAP2 in cultured cerebeller macroneurons inhibits minor neurite formation
Cáceres, A., Mautino, J., & Kosik, K. S. (1992) · Neuron · doi:10.1016/0896-6273(92)90025-9 · Cited by 256 · see citing works
Self-citation
The interaction of actin filaments with microtubules and microtubule-associated proteins.
Griffith, L. M., & Pollard, T. D. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34254-6 · Cited by 252 · see citing works
Tension and compression in the cytoskeleton of PC 12 neurites.
Joshi, H. C., Chu, D., Buxbaum, R. E., & Heidemann, S. R. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.3.697 · Cited by 224 · see citing works
Microtubule behavior during guidance of pioneer neuron growth cones in situ.
Sabry, J. H., O’Connor, T. P., Evans, L., Toroian‐Raymond, A., Kirschner, M. W., & Bentley, D. (1991) · The Journal of Cell Biology · doi:10.1083/jcb.115.2.381 · Cited by 216 · see citing works
Differences in the organization of actin in the growth cones compared with the neurites of cultured neurons from chick embryos.
Letourneau, P. C. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.97.4.963 · Cited by 214 · see citing works
Identification of fodrin as a major calmodulin-binding protein in postsynaptic density preparations.
Carlin, R. K., Bartelt, D. C., & Siekevitz, P. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.96.2.443 · Cited by 204 · see citing works
Phosphorylation determines the binding of microtubule-associated protein 2 (MAP2) to microtubules in living cells.
Brugg, B., & Matus, A. I. (1991) · The Journal of Cell Biology · doi:10.1083/jcb.114.4.735 · Cited by 199 · see citing works
Mammalian brain phosphoproteins as substrates for calcineurin.
King, M. M., Huang, C., Chock, P. B., Nairn, A. C., Hemmings, H. C., Chan, K.-F. J., & Greengard, P. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39694-1 · Cited by 198 · see citing works
Ca2+, Calmodulin‐Dependent Regulation of Microtubule Formation via Phosphorylation of Microtubule‐Associated Protein 2, τ Factor, and Tubulin, and Comparison with the Cyclic AMP‐Dependent Phosphorylation
Yamamoto, H., Fukunaga, K., Goto, S., Tanaka, E., & Miyamoto, E. (1985) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1985.tb12880.x · Cited by 180 · see citing works
Dephosphorylation of Microtubule‐Associated Protein 2, τ Factor, and Tubulin by Calcineurin
Goto, S., Yamamoto, H., Fukunaga, K., Iwasa, T., Matsukado, Y., & Miyamoto, E. (1985) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1985.tb05504.x · Cited by 178 · see citing works
Growth cone formation in cultures of sensory neurons.
Bray, D., Thomas, C., & Shaw, G. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.10.5226 · Cited by 167 · see citing works
Cyclosporin-mediated inhibition of bovine calcineurin by cyclophilins A and B.
Swanson, S., Born, T. L., Zydowsky, L. D., Cho, H., Chang, H. Y., Walsh, C. T., & Rusnak, F. M. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.9.3741 · Cited by 165 · see citing works
Cloning of human calcineurin A: evidence for two isozymes and identification of a polyproline structural domain.
Guerini, D., & Klee, C. B. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.23.9183 · Cited by 165 · see citing works
Microtubule-associated proteins (MAPs) and the organization of actin filaments in vitro.
Sattilaro, R. F., Dentler, W. L., & LeCluyse, E. L. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.90.2.467 · Cited by 164 · see citing works
Dephosphorylation of Neuromodulin by Calcineurin
Liu, Y., & Storm, D. R. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)51557-x · Cited by 160 · see citing works
Microtubule formation and neurite growth in cerebellar macroneurons which develop in vitro: evidence for the involvement of the microtubule-associated proteins, MAP-1a, HMW-MAP2 and Tau
Ferreira, A., Busciglio, J. A., & Cáceres, A. (1989) · Developmental Brain Research · doi:10.1016/0165-3806(89)90023-0 · Cited by 151 · see citing works
Self-citation
Processes induced by tau expression in Sf9 cells have an axon-like microtubule organization.
Baas, P. W., Pienkowski, T. P., & Kosik, K. S. (1991) · The Journal of Cell Biology · doi:10.1083/jcb.115.5.1333 · Cited by 143 · see citing works
Self-citation
Occurrence of caldesmon (a calmodulin-binding protein) in cultured cells: comparison of normal and transformed cells.
Owada, M. K., Hakura, A., Iida, K., Yahara, I., Sobue, K., & Kakiuchi, S. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.10.3133 · Cited by 140 · see citing works
Spectrin subtypes in mammalian brain: an immunoelectron microscopic study
Zagon, I., Higbee, R. G., Riederer, B. M., & Goodman, S. R. (1986) · Journal of Neuroscience · doi:10.1523/jneurosci.06-10-02977.1986 · Cited by 136 · see citing works
Calcineurin
Klee, C. B., Draetta, G. F., & Hubbard, M. J. (1988) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123072.ch4 · Cited by 135 · see citing works
Cloning and characterization of molecular isoforms of the catalytic subunit of calcineurin using nonisotopic methods.
Kincaid, R. L., Giri, P. R., Higuchi, S., Tamura, J., DIXON, S. C., Marietta, C. A., Amorese, D. A., & Martin, B. M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38593-x · Cited by 131 · see citing works
Self-citation
Phosphorylation of Microtubule-Associated Proteins (MAPs) and pH of the Medium Control Interaction between MAPs and Actin Filaments1
Nishida, E., Kuwaki, T., & Sakai, H. (1981) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a133510 · Cited by 116 · see citing works
The role of cytoskeleton in organizing growth cones: a microfilament-associated growth cone component depends upon microtubules for its localization.
Goslin, K., Birgbauer, E., Banker, G. A., & Solomon, F. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.4.1621 · Cited by 106 · see citing works
Cytochalasin separates microtubule disassembly from loss of asymmetric morphology.
Solomon, F., & Magendantz, M. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.89.1.157 · Cited by 103 · see citing works
Concentration of membrane antigens by forward transport and trapping in neuronal growth cones
Sheetz, M. P., Baumrind, N. L., Wayne, D. B., & Pearlman, A. L. (1990) · Cell · doi:10.1016/0092-8674(90)90804-n · Cited by 95 · see citing works
Differential localization of calmodulin-dependent enzymes in rat brain: evidence for selective expression of cyclic nucleotide phosphodiesterase in specific neurons.
Kincaid, R. L., Balaban, C. D., & Billingsley, M. L. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.4.1118 · Cited by 94 · see citing works
Self-citation
Molecular cloning of a calmodulin-dependent phosphatase from murine testis: identification of a developmentally expressed nonneural isoenzyme.
Muramatsu, T., Giri, P. R., Higuchi, S., & Kincaid, R. L. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.2.529 · Cited by 85 · see citing works
Self-citation
Structure and expression of two isoforms of the murine calmodulin-dependent protein phosphatase regulatory subunit (calcineurin B)
Ueki, K., Muramatsu, T., & Kincaid, R. L. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)81527-x · Cited by 76 · see citing works
Self-citation
The expression of acetylated microtubules during axonal and dendritic growth in cerebellar macroneurons which develop in vitro
Ferreira, A., & Cáceres, A. (1989) · Developmental Brain Research · doi:10.1016/0165-3806(89)90022-9 · Cited by 75 · see citing works
Self-citation
Regulation of organelle transport in melanophores by calcineurin.
Thaler, C. D., & Haimo, L. T. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.111.5.1939 · Cited by 75 · see citing works
Dephosphorylation of r Factor by Protein Phosphatase 2A in Synaptosomal Cytosol Fractions, and Inhibition by Aluminum
Yamamoto, H., Saitoh, Y., Yasugawa, S., & Miyamoto, E. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb04187.x · Cited by 73 · see citing works
Purification and properties of calmodulin-stimulated phosphodiesterase from mammalian brain.
Kincaid, R. L., Manganiello, V., Odya, C. E., Osborne, J. C., Stith-Coleman, I., Danello, M. A., & Vaughan, M. J. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42970-x · Cited by 71 · see citing works
Self-citation
Polarized compartmentalization of organelles in growth cones from developing optic tectum.
Cheng, T. P. ‐., & Reese, T. S. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.4.1473 · Cited by 69 · see citing works
Local role of Ca2+ in formation of veils in growth cones
Goldberg, D. (1988) · Journal of Neuroscience · doi:10.1523/jneurosci.08-07-02596.1988 · Cited by 67 · see citing works
Expression of the calmodulin-dependent protein phosphatase, calcineurin, in rat brain: developmental patterns and the role of nigrostriatal innervation
Polli, J. W., Billingsley, M. L., & Kincaid, R. L. (1991) · Developmental Brain Research · doi:10.1016/0165-3806(91)90071-p · Cited by 63 · see citing works
Self-citation
Calmodulin-binding proteins that interact with actin filaments in a Ca2+-dependent flip-flop manner: survey in brain and secretory tissues.
Sobue, K., Kanda, K., Adachi, J., & Kakiuchi, S. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.22.6868 · Cited by 63 · see citing works
Calmodulin-dependent protein phosphatase: a developmental study
Tallant, E. A., & Cheung, W. Y. (1983) · Biochemistry · doi:10.1021/bi00284a014 · Cited by 56 · see citing works
Calcineurin in human brain and its relation to extrapyramidal system
Goto, S., Matsukado, Y., Mihara, Y., Inoue, N., & Miyamoto, E. (1986) · Acta Neuropathologica · doi:10.1007/bf00685977 · Cited by 42 · see citing works
An actin-associated protein present in the microtubule organizing center and the growth cones of PC-12 cells
Bearer, E. L. (1992) · Journal of Neuroscience · doi:10.1523/jneurosci.12-03-00750.1992 · Cited by 31 · see citing works
[57] Preparation, characterization, and properties of affinity-purified antibodies to calmodulin-dependent cyclic nucleotide phosphodiesterase and the protein phosphatase calcineurin
Kincaid, R. L. (1988) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(88)59059-6 · Cited by 29 · see citing works
Self-citation
The Interaction between Calmodulin and Microtubule Proteins. IV. Quantitative Analysis of the Binding between Calmodulin and Tubulin Dimer1
KUMAGAI, H., Nishida, E., & Sakai, H. (1982) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a133819 · Cited by 25 · see citing works
Ca2+ and calmodulin regulate microtubule-associated protein-actin filament interaction in a flip-flop switch
Sobue, K., Tanaka, T. P., Ashino, N., & Kakiuchi, S. (1985) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(85)90200-9 · Cited by 24 · see citing works

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Rusnak, F. M., & Mertz, P. S. (2000) · Physiological Reviews · doi:10.1152/physrev.2000.80.4.1483 · Cited by 1,375 · see citing works
Tau is essential to β-amyloid-induced neurotoxicity
Rapoport, M., Dawson, H. N., Binder, L. I., Vitek, M. P., & Ferreira, A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092136199 · Cited by 807 · see citing works
Self-citation
Phosphorylation of microtubule-associated protein 2 (MAP2) and its relevance for the regulation of the neuronal cytoskeleton function
Sánchez, C. (2000) · Progress in Neurobiology · doi:10.1016/s0301-0082(99)00046-5 · Cited by 512 · see citing works
Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration.
Billingsley, M., & Kincaid, R. (1997) · Biochemical Journal · doi:10.1042/bj3230577 · Cited by 469 · see citing works
Self-citation
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Halpain, S., Hipolito, A., & Saffer, L. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-23-09835.1998 · Cited by 408 · see citing works
“In developing cerebellar (Ferreira et al., 1993) and hippocampal (Halpain et al., 1997) neurons, calcineurin is highly concentrated in growth cones, structures that, like spines, contain a dense network of F-actin.”
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Steinbach, W. J., Cramer, R. A., Perfect, B. Z., Asfaw, Y. G., Sauer, T. C., Najvar, L. K., Kirkpatrick, W. R., Patterson, T. F., Benjamin, D. K., Heitman, J., et al. (2006) · Eukaryotic Cell · doi:10.1128/ec.00139-06 · Cited by 264 · see citing works
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Kempf, M., Clement, A. M., Faissner, A., Lee, G. S., & Brandt, R. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-18-05583.1996 · Cited by 248 · see citing works
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Hemenway, C. S., & Heitman, J. (1999) · Cell Biochemistry and Biophysics · doi:10.1007/bf02737887 · Cited by 227 · see citing works
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Lee, S. C., Li, A., Calo, S., & Heitman, J. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003625 · Cited by 172 · see citing works
Identification and characterization of a highly conserved calcineurin binding protein, CBP1/calcipressin, in Cryptococcus neoformans
Görlach, J. M., Fox, D. S., Cutler, N. S., Cox, G. M., Perfect, J. R., & Heitman, J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.14.3618 · Cited by 172 · see citing works
Regulation of Calcineurin by Growth Cone Calcium Waves Controls Neurite Extension
Lautermilch, N. J., & Spitzer, N. C. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-01-00315.2000 · Cited by 164 · see citing works
Calcineurin: Not Just a Simple Protein Phosphatase
Guerini, D. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6802 · Cited by 156 · see citing works
Asymmetric retraction of growth cone filopodia following focal inactivation of calcineurin
Chang, H. Y., Takei, K., Sydor, A. M., Born, T. L., Rusnak, F. M., & Jay, D. G. (1995) · Nature · doi:10.1038/376686a0 · Cited by 155 · see citing works
Calcineurin is required for hyphal elongation during mating and haploid fruiting in Cryptococcus neoformans
Cruz, M. C., Fox, D. S., & Heitman, J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.5.1020 · Cited by 150 · see citing works
Good fungi gone bad: The corruption of calcineurin
Fox, D. S., & Heitman, J. (2002) · BioEssays · doi:10.1002/bies.10157 · Cited by 137 · see citing works
Activated calcineurin confers high tolerance to ion stress and alters the budding pattern and cell morphology of yeast cells
Mendoza, I., Quintero, F. J., Bressan, R. A., Hasegawa, P. M., & Pardo, J. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23061 · Cited by 115 · see citing works
Exogenous BDNF, NT-3 and NT-4 differentially regulate neurite outgrowth in cultured hippocampal neurons
Labelle, C., & Leclerc, N. M. (2000) · Developmental Brain Research · doi:10.1016/s0165-3806(00)00069-9 · Cited by 110 · see citing works
Don’t get too excited: mechanisms of glutamate-mediated Purkinje cell death
Slemmer, J. E., De Zeeuw, C. I., & Weber, J. T. (2005) · Progress in Brain Research · doi:10.1016/s0079-6123(04)48029-7 · Cited by 108 · see citing works
Antifungal Activities of Antineoplastic Agents: Saccharomyces cerevisiae as a Model System To Study Drug Action
Cardenas, M. E., Cruz, M. C., Poeta, M. D., Chung, N., Perfect, J. R., & Heitman, J. (1999) · Clinical Microbiology Reviews · doi:10.1128/cmr.12.4.583 · Cited by 103 · see citing works
Cytoskeletal Changes in the Brains of Mice Lacking Calcineurin Aα
Kayyali, U. S., Zhang, W., Yee, A. G., Seidman, J. G., & Potter, H. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68041668.x · Cited by 99 · see citing works
Differential effects of olanzapine on the gene expression of superoxide dismutase and the low affinity nerve growth factor receptor
Li, X., Chlan‐Fourney, J., Juorio, A. V., Bennett, V. L., Shrikhande, S., Keegan, D. L., Jin, Q., & Boulton, A. A. (1999) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19990401)56:1 · Cited by 57 · see citing works
Microtubule-associated Protein 2c Reorganizes Both Microtubules and Microfilaments into Distinct Cytological Structures in an Actin-binding Protein-280–deficient Melanoma Cell Line
Cunningham, C. C., Leclerc, N., Flanagan, L. A., Lu, M., Janmey, P. A., & Kosik, K. S. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.4.845 · Cited by 88 · see citing works
Self-citation
Calcium-stimulated Phosphorylation of MAP-2 in Pancreatic TC3-cells Is Mediated by Ca2+/Calmodulin-dependent Kinase II
Krueger, K. A., Bhatt, H. S., Landt, M., & Easom, R. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.43.27464 · Cited by 86 · see citing works
Regulation of Actin Tension in Plant Cells by Kinases and Phosphatases1
Grabski, S., Arnoys, E. J., Busch, B., & Schindler, M. (1998) · PLANT PHYSIOLOGY · doi:10.1104/pp.116.1.279 · Cited by 80 · see citing works
Modulation of the phosphorylation state of tau in situ: the roles of calcium and cyclic AMP
Fleming, L. M., & Johnson, G. V. W. (1995) · Biochemical Journal · doi:10.1042/bj3090041 · Cited by 80 · see citing works
CAMs and FGF cause a local submembrane calcium signal promoting axon outgrowth without a rise in bulk calcium concentration
Archer, F., Doherty, P., Collins, D., & Bolsover, S. R. (1999) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.1999.00773.x · Cited by 77 · see citing works
Immunophilin Ligands and GDNF Enhance Neurite Branching or Elongation from Developing Dopamine Neurons in Culture
Costantini, L. C., & Ole Isacson, A. (2000) · Experimental Neurology · doi:10.1006/exnr.2000.7417 · Cited by 77 · see citing works
Growth Cones Are Not Required for Initial Establishment of Polarity or Differential Axon Branch Growth in Cultured Hippocampal Neurons
Ruthel, G. T., & Hollenbeck, P. J. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-06-02266.2000 · Cited by 68 · see citing works
The protein serine/threonine phosphatases PP2A, PP1 and calcineurin: A triple threat in the regulation of the neuronal cytoskeleton
Hoffman, A., Taleski, G., & Sontag, E. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.01.005 · Cited by 65 · see citing works
Structure, chromosomal localization, and brain expression of human Cx36 gene
Belluardo, N., Salinaro, A. T., Mudò, G., Hurd, Y. L., & Condorelli, D. F. (1999) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19990901)57:5 · Cited by 110 · see citing works
Regulation of vascular endothelial cell barrier function and cytoskeleton structure by protein phosphatases of the PPP family
Csoŕtos, C., Kolosova, I. A., & Verin, A. D. (2007) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00120.2007 · Cited by 62 · see citing works
Accelerated neuronal differentiation induced by p53 suppression
Ferreira, A., & Kosik, K. S. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.6.1509 · Cited by 59 · see citing works
Self-citation
Post-translational modifications of tau protein
Pevalova, M., Filipčík, P., Novák, M., Ávila, J., & Iqbal, K. (2006) · Bratislavské lekárske listy/Bratislava medical journal · doi:10.1007/bf03656852 · Cited by 52 · see citing works
Identified motor terminals inDrosophila larvae show distinct differences in morphology and physiology
Lnenicka, G. A., & Keshishian, H. (2000) · Journal of Neurobiology · doi:10.1002/(sici)1097-4695(200005)43:2 · Cited by 142 · see citing works
Molecules, Signaling, and Schizophrenia
Kvajo, M., McKellar, H., & Gogos, J. A. (2010) · Current topics in behavioral neurosciences · doi:10.1007/7854_2010_41 · Cited by 48 · see citing works
The tau proteins in neuronal growth and development
Brandt, R. (1996) · Frontiers in bioscience · doi:10.2741/a120 · Cited by 47 · see citing works
Role of Ca2+/calmodulin-dependent phosphatase 2B in thrombin-induced endothelial cell contractile responses
Verin, A. D., Cooke, C., Herenyiova, M., Patterson, C. E., & Garcia, J. G. N. (1998) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1998.275.4.l788 · Cited by 44 · see citing works
Inhibition of protein phosphatase-2B (calcineurin) activity towards Alzheimer abnormally phosphorylated τ by neuroleptics
Gong, C., Shaikh, S., Grundke, I., & Iqbal, K. (1996) · Brain Research · doi:10.1016/s0006-8993(96)00904-3 · Cited by 44 · see citing works
Myristoylation of Calcineurin B Is Not Required for Function or Interaction with Immunophilin-Immunosuppressant Complexes in the Yeast Saccharomyces cerevisiae
Zhu, D., Cardenas, M. E., & Heitman, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.42.24831 · Cited by 43 · see citing works
An Analysis of an Axonal Gradient of Phosphorylated MAP 1B in Cultured Rat Sensory Neurons
Bush, M. S., Goold, R., Moya, F., & Gordon‐Weeks, P. R. (1996) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1996.tb01208.x · Cited by 42 · see citing works
Aspergillus fumigatus Calcipressin CbpA Is Involved in Hyphal Growth and Calcium Homeostasis
Pinchai, N., Perfect, B. Z., Juvvadi, P. R., Fortwendel, J. R., Cramer, R. A., Asfaw, Y. G., Heitman, J., Perfect, J. R., & Steinbach, W. J. (2009) · Eukaryotic Cell · doi:10.1128/ec.00336-08 · Cited by 41 · see citing works
Expression and subcellular localization of Ror tyrosine kinase receptors are developmentally regulated in cultured hippocampal neurons
Paganoni, S., & Ferreira, A. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10674 · Cited by 41 · see citing works
Self-citation
Reduction of calcineurin activity in brain by antisense oligonucleotides leads to persistent phosphorylation of tau protein at Thr181 and Thr231.
Garver, T. D., Kincaid, R. L., Conn, R. A., & Billingsley, M. L. (1999) · PubMed · Cited by 40 · see citing works
Self-citation
Neuroprotective signal transduction in model motor neurons exposed to thrombin: G‐protein modulation effects on neurite outgrowth, Ca2 mobilization, and apoptosis
Smirnova, I. V., Citron, B. A., Arnold, P. M., & Festoff, B. W. (2001) · Journal of Neurobiology · doi:10.1002/neu.1044.abs · Cited by 40 · see citing works
Calcineurin dephosphorylates the C-terminal region of filamin in an important regulatory site: A possible mechanism for filamin mobilization and cell signaling
García, E., Stracher, A., & Jay, D. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.12.006 · Cited by 39 · see citing works
Differential expression of members of the RCAN family of calcineurin regulators suggests selective functions for these proteins in the brain
Porta, S., Martı́, E., de la Luna, S., & Arbonés, M. L. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05749.x · Cited by 38 · see citing works
Calcineurin-dependent cofilin activation and increased retrograde actin flow drive 5-HT–dependent neurite outgrowth inAplysiabag cell neurons
Zhang, X., Hyland, C., Goor, D. V., & Forscher, P. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0715 · Cited by 37 · see citing works
Role of Ca++/Calmodulin binding proteins in Aspergillus nidulans cell cycle regulation
Nanthakumar, N. N., Dayton, J. S., & Means, A. R. (1996) · Springer eBooks · doi:10.1007/978-1-4615-5873-6_21 · Cited by 35 · see citing works
Interneurons of the ganglionic layer in the mormyrid electrosensory lateral line lobe: Morphology, immunohistochemistry, and synaptology
Meek, J., Grant, K., Sugawara, Y., Hafmans, T. G. M., Ravaille‐Veron, M., & Denizot, J. (1996) · The Journal of Comparative Neurology · doi:10.1002/(sici)1096-9861(19961104)375:1 · Cited by 50 · see citing works
Site-specific regulation of Alzheimer-like tau phosphorylation in living neurons
Burack, M. A., & Halpain, S. (1996) · Neuroscience · doi:10.1016/0306-4522(95)00546-3 · Cited by 34 · see citing works
Functional repertoire of protein kinases and phosphatases in synaptic plasticity and associated neurological disorders
Kulasiri, D., Khan, R., & Samarasinghe, S. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.300331 · Cited by 33 · see citing works
Calcineurin regulation of cytoskeleton organization: a new paradigm to analyse the effects of calcineurin inhibitors on the kidney
Descazeaud, V., Mestre, E., Marquet, P., & Essig, M. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01398.x · Cited by 32 · see citing works
Facial motor neuron regeneration induces a unique spatial and temporal pattern of myristoylated alanine-rich C kinase substrate expression
McNamara, R. K., Jiang, Y., Streit, W. J., & Lenox, R. H. (2000) · Neuroscience · doi:10.1016/s0306-4522(00)00039-7 · Cited by 32 · see citing works
Acute rise in the concentration of free cytoplasmic calcium leads to dephosphorylation of the microtubule-associated protein tau
Adamec, E., Mercken, M. H., Beermann, M. L., Didier, M., & Nixon, R. A. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00166-2 · Cited by 32 · see citing works
Treatment of hippocampal neurons with cyclosporin A results in calcium overload and apoptosis which are independent on NMDA receptor activation
Kaminska, B., Figiel, I., Pyrzyńska, B., Czajkowski, R., & Mosieniak, G. (2001) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0704177 · Cited by 30 · see citing works
Variations in in vivo phosphorylation at the proline-rich domain of the microtubule-associated protein 2 (MAP2) during rat brain development
Sánchez, C., Díaz‐Nido, J., & Ávila, J. (1995) · Biochemical Journal · doi:10.1042/bj3060481 · Cited by 29 · see citing works
Stress-Induced Tau Phosphorylation in Mouse Strains with Different Brain Erk 1 + 2 Immunoreactivity
Korneyev, A. (1998) · Neurochemical Research · doi:10.1023/a:1020980004539 · Cited by 28 · see citing works
Secreted β-APP stimulates MAP kinase and phosphorylation of tau in neurons
Greenberg, S. M., & Kosik, K. S. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(94)00172-w · Cited by 28 · see citing works
Self-citation
Short- and long-term mechanisms of tau regulation in PC12 cells
Sadot, E., Barg, J., Rasouly, D., Lazarovici, P., & Ginzburg, I. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.8.2857 · Cited by 25 · see citing works
Estrogen-induced changes in the microtubular system correlate with a decreased susceptibility of aging neurons to beta amyloid neurotoxicity
Shah, R. M. (2003) · Molecular and Cellular Neuroscience · doi:10.1016/s1044-7431(03)00166-0 · Cited by 25 · see citing works
In VivoCalcium Signaling during Synaptic Refinement at theDrosophilaNeuromuscular Junction
Vonhoff, F., & Keshishian, H. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2922-16.2017 · Cited by 22 · see citing works
Developmental changes in the regulation of calcium-dependent neurite outgrowth
Arie, Y., Iketani, M., Takamatsu, K., Mikoshiba, K., Goshima, Y., & Takei, K. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.11.128 · Cited by 23 · see citing works
Reduction of Calcineurin Activity in Brain by Antisense Oligonucleotides Leads to Persistent Phosphorylation of τ Protein at Thr181 and Thr231
Garver, T. D., Kincaid, R. L., Conn, R. A., & Billingsley, M. L. (1999) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)23024-8 · Cited by 23 · see citing works
Self-citation
Immunosuppressant FK506 prevents mossy fiber sprouting induced by kindling stimulation
Moriwaki, A., Lü, Y.-F., Hayashi, Y., Tomizawa, K., Tokuda, M., Itano, T., Hatase, O., & Matsui, H. (1996) · Neuroscience Research · doi:10.1016/0168-0102(96)01036-x · Cited by 23 · see citing works
Postnatal changes in serine/threonine protein phosphatases and their association with the microtubules
Dudek, S. M., & Johnson, G. V. W. (1995) · Developmental Brain Research · doi:10.1016/0165-3806(96)83486-9 · Cited by 23 · see citing works
Signal Transducer and Activator of Transcription 3 (STAT3) Degradation by Proteasome Controls a Developmental Switch in Neurotrophin Dependence
Murase, S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.470583 · Cited by 21 · see citing works
Zinc in Regulating Protein Kinases and Phosphatases in Neurodegenerative Diseases
Zhang, H.-L., Wang, X., & Liu, R. (2022) · Biomolecules · doi:10.3390/biom12060785 · Cited by 20 · see citing works
The role of calcineurin in immune system responses
Kincaid, R. L. (1995) · Journal of Allergy and Clinical Immunology · doi:10.1016/s0091-6749(95)70202-4 · Cited by 20 · see citing works
Self-citation
Calcineurin expression and localisation during porcine oocyte growth and meiotic maturation
Tůmová, L., Petr, J., Žalmanová, T., Chmelíková, E., Kott, T., Tichovská, H., Kučerová-Chrpová, V., Hošková, K., & Jílek, F. (2013) · Animal Reproduction Science · doi:10.1016/j.anireprosci.2013.07.011 · Cited by 19 · see citing works
Direct measurement of local raised subplasmalemmal calcium concentrations in growth cones advancing on an N‐cadherin substrate
Chadborn, N., Eickholt, B. J., Doherty, P., & Bolsover, S. R. (2002) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2002.02033.x · Cited by 18 · see citing works
NMDA receptors inhibit axonal outgrowth by inactivating Akt and activating GSK-3β via calcineurin in cultured immature hippocampal neurons
Wang, Y., Tang, J.-L., Xu, X., Zhou, X., Du, J., Wang, X., Zhou, Y., Zhu, Q., Yao, L., Wang, Y., et al. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.08.033 · Cited by 15 · see citing works
Seven cDNAs enriched following hippocampal lesion: possible roles in neuronal responses to injury
Price, M., Lang, M., Frank, A. T., Goetting‐Minesky, M. P., Patel, S. P., Silviera, M. L., Krady, J. K., Milner, R. J., Ewing, A. G., & Day, J. R. (2003) · Molecular Brain Research · doi:10.1016/s0169-328x(03)00285-7 · Cited by 16 · see citing works
The Rate of Tau Synthesis Is Differentially Regulated During Postnatal Development in Mouse Cerebellum
Vilá‐Ortíz, G. J., Santa-Coloma, T. A., Carminatti, H., & Radrizzani, M. (2001) · Cellular and Molecular Neurobiology · doi:10.1023/a:1013823524302 · Cited by 15 · see citing works
[42] Strategies to assess phosphoprotein phosphatase and protein kinase-mediated regulation of the cytoskeleton
Eriksson, J., Toivola, D. M., Sahlgren, C., Mikhailov, A., & Härmälä-Braskén, A.-S. (1998) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(98)98044-2 · Cited by 15 · see citing works
Airway nerves and protein phosphatases
Harrison, S., Page, C. P., & Spina, D. (1999) · General Pharmacology The Vascular System · doi:10.1016/s0306-3623(98)00204-3 · Cited by 15 · see citing works
Prolonged infusion of inhibitors of calcineurin or L‐type calcium channels does not block mossy fiber sprouting in a model of temporal lobe epilepsy
Ingram, E. A., Toyoda, I., Wen, X., & Buckmaster, P. S. (2008) · Epilepsia · doi:10.1111/j.1528-1167.2008.01704.x · Cited by 13 · see citing works
Immunosuppressants FK506 and rapamycin have different effects on the biosynthesis of cytoplasmic actin during the early period of T cell activation
Miyamoto, S., & Safer, B. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3440803 · Cited by 13 · see citing works
Interruption of T‐cell signal transduction by lentivirus lytic peptides from HIV‐1 transmembrane protein
Beary, T. P., Tencza, S. B., Mietzner, T. A., & Montelaro, R. C. (1998) · Journal of Peptide Research · doi:10.1111/j.1399-3011.1998.tb00419.x · Cited by 12 · see citing works
Biochemistry and Pharmacology of Calmodulin-Regulated Phosphatase Calcineurin
Perrino, B. A., & Soderling, T. R. (1998) · Elsevier eBooks · doi:10.1016/b978-0-08-092636-0.50008-6 · Cited by 11 · see citing works
A Calcineurin Regulator MoRCN1 Is Important for Asexual Development, Stress Response, and Plant Infection of Magnaporthe oryzae
Liu, C., Liu, T., Lv, Z., Qin, M., Qu, Z., Zhang, Z., Li, F., Chen, D., Zhang, X., Chen, X., et al. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.925645 · Cited by 8 · see citing works
Effect of cyclosporine on anterior chamber-associated immune deviation with retinal transplantation.
Ishioka, M., Okamoto, S., Streilein, J. W., & Jiang, L. Q. (1997) · PubMed · Cited by 8 · see citing works
Identification of calcineurin as a predictor of oocyte quality and fertilization competence based on microarray data
Daei-farshbaf, N., Aflatoonian, R., Amjadi, F., Nikniaz, H., Taleahmad, S., & Bakhtiyari, M. (2021) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2021.107561 · Cited by 8 · see citing works
Calcium and Neuronal Development and Growth
Archer, F., Ashworth, R., & Bolsover, S. R. (1998) · Springer eBooks · doi:10.1007/978-1-4899-1901-4_12 · Cited by 8 · see citing works
Differential synthesis and cytoskeletal deposition of neurofilament subunits before and during axonal outgrowth in NB2a/d1 cells: Evidence that segregation of phosphorylated subunits within the axonal cytoskeleton involves selective deposition
Shea, T. B. (1995) · Journal of Neuroscience Research · doi:10.1002/jnr.490400211 · Cited by 8 · see citing works
Role of calcineurin in thrombin‐mediated endothelial cell contraction
Kolozsvári, B., Szíjgyártó, Z., Bai, P., Gergely, P., Verin, A. D., Garcia, J. G. N., & Bakó, É. (2009) · Cytometry Part A · doi:10.1002/cyto.a.20707 · Cited by 7 · see citing works
Calcineurin inhibition may prevent Alzheimer disease in people with Down syndrome
Dohl, J., Treadwell, Z., Norris, C. M., & Head, E. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70034 · Cited by 6 · see citing works
Potential role of calcineurin in pathogenic conditions
Kurji, K. H., & Sharma, R. K. (2009) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-009-0346-4 · Cited by 6 · see citing works
Synergy of Cytoskeleton Components
Gavin, R. H. (1999) · BioScience · doi:10.2307/1313440 · Cited by 4 · see citing works
La3+ stimulate the activity of calcineurin in two different ways
Hu, J., Yang, X., & Wang, K. (2005) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-005-0021-5 · Cited by 3 · see citing works
Calcineurin is an adaptor required for assembly of the TCR signaling complex
Otsuka, S., Dutta, D., Wu, C.-J., Alam, M. S., & Ashwell, J. D. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114568 · Cited by 2 · see citing works
Influence of phosphorylation on isoform composition and function of a microtubule-associated protein from developing Artemia
Zhang, J., & MacRae, T. H. (1995) · Biochemical Journal · doi:10.1042/bj3070419 · Cited by 2 · see citing works
Low-frequency electromagnetic fields influence the expression of calcium metabolism related proteins in leukocytic cell lines
Wójcik‐Piotrowicz, K., Kaszuba-Zwoińska, J., Piszczek, P., Nowak, B., Guzdek, P., Gil, K., & Rokita, E. (2023) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2023.104320 · Cited by 1 · see citing works
Calcineurin as a Pivotal Ca2+-Sensitive Switching Element in Biological Responses: Implications for the Regulation of Tau Phosphorylation in Alzheimer’s Disease
Kincaid, R. L. (1995) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-79423-0_9 · Cited by 1 · see citing works
Self-citation
Protein Kinases and Phosphatases in Cellular Signaling
Leach, K. L. (1998) · Comprehensive physiology · doi:10.1002/cphy.cp070110 · Cited by 1 · see citing works
Effect on protein phosphatase activity of peptide backbone modification and truncation of the autoinhibitory domain peptide of calcineurin
Bannow, C. A., Staples, D. J., Smith, C. W., Chapman, D. L., & Leach, K. L. (1996) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1996.tb00815.x · Cited by 1 · see citing works
Linking Amyloid Precursor Protein Processing and Tau-Related Pathology in Alzheimer’s Disease
Kosik, K. S., Ferreira, A., Knowles, R. B., Leclerc, N. M., & Greenberg, S. M. (1995) · Springer eBooks · doi:10.1007/978-3-642-79423-0_19 · Cited by 1 · see citing works
Self-citation
Calcineurin
Kamaldeen Muili, A. O. (2011) · doi:10.3998/panc.2011.4 · Cited by 1 · see citing works
Identification of Novel Genes Critical for CNS Regeneration in L. stagnalis
Aleksic, M. (2011) · TSpace (University of Toronto)
Modifications du cytosquelette des cellules tubulaires proximales rénales par les inhibiteurs de la calcineurine : rôle dans la dysfonction chronique du greffon
de Merindol-Descazeaud, V. (2011)
Tau phosphorylation and neurite extension: Different phosphorylation sites, different protein kinases, different consequences
Ávila, J. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(94)00167-y

Calcineurin localization at the growing tips of neurites depends upon intact cytoskeletal components
Ferreira, A., Kincaid, R. L., & Kosik, K. S. (1992)
Self-citation
Regulation of Calcineurin by Growth Cone Calcium Waves Controls Neurite Extension
Lautermilch, N. J., & Spitzer, N. C. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-01-00315.2000 · Cited by 164 · see citing works
Asymmetric retraction of growth cone filopodia following focal inactivation of calcineurin
Chang, H. Y., Takei, K., Sydor, A. M., Born, T. L., Rusnak, F. M., & Jay, D. G. (1995) · Nature · doi:10.1038/376686a0 · Cited by 155 · see citing works
Cyclosporin A promotes axon growth of cortical neurons by inhibiting calcineurin activity
Zhang, L. (2007) · Di-san junyi daxue xuebao
The microtubule cytoskeleton and the development of neuronal polarity
Mandell, J. W., & Banker, G. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(94)00164-v · Cited by 68 · see citing works

Authors: Ferreira, A., Kincaid, R., & Kosik, K. S.
Affiliations: Harvard University (US)
ORCID: Ferreira, A
Kosik, K S
Venue: Molecular Biology of the Cell
Publisher: American Society for Cell Biology (ASCB)
Published: 1993-12
Volume: 4
Issue: 12
Pages: 1225-1238
ISSN: 1059-1524 (ISSN-L)
1939-4586
DOI: 10.1091/mbc.4.12.1225
PMC: PMC275760
OpenAlex: W2092619158
Cited by: 110
References: 74
Citations by year: 2026: 1 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 1 · 2020: 1 · 2018: 1 · 2017: 2 · 2016: 1 · 2015: 1 · 2013: 3 · 2012: 2
FWCI: 3.01
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Molecular Biology of the Cell (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01ag006601-13, 5r01ns029031-09)
National Institute on Aging (AG 06601)
National Institute of Neurological Disorders and Stroke (NS29031)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Keywords: calcineurin, neuronal polarity, neurite outgrowth, growth cones, microtubules, F-actin, tau phosphorylation, cyclosporine, cerebellar neurons, axon elongation
MeSH terms: Animals, Calmodulin-Binding Proteins, Cell Differentiation, Cells, Cultured, Cerebellum, Cytoskeleton, Actin Cytoskeleton, Microtubules, Nerve Tissue Proteins, Neurons, Phosphoprotein Phosphatases, Phosphorylation, Protein Processing, Post-Translational, Cytochalasin D, Nocodazole, Neurites, Cyclosporine, Cell Polarity, tau Proteins, Calcineurin, Rats

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Calcineurin is associated with the cytoskeleton of cultured neurons and has a role in the acquisition of polarity.

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