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Transport of CaM kinase along processes elicited by neuronal contact evokes an inhibition of arborization and outgrowth in D. melanogaster cultured neurons

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Transport of CaM kinase along processes elicited by neuronal contact evokes an inhibition of arborization and outgrowth in D. melanogaster cultured neurons. / Broughton, S J; Kane, N S; Yoder, M; Greenspan, R J; Robichon, A.

In: Journal of Cellular Biochemistry, Vol. 62, No. 4, 15.09.1996, p. 484-494.

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Broughton, S J ; Kane, N S ; Yoder, M ; Greenspan, R J ; Robichon, A. / Transport of CaM kinase along processes elicited by neuronal contact evokes an inhibition of arborization and outgrowth in D. melanogaster cultured neurons. In: Journal of Cellular Biochemistry. 1996 ; Vol. 62, No. 4. pp. 484-494.

Bibtex

@article{a924ad45cf384b1abe20748bdb327f58,
title = "Transport of CaM kinase along processes elicited by neuronal contact evokes an inhibition of arborization and outgrowth in D. melanogaster cultured neurons",
abstract = "Transgenic Drosophila strains expressing an inhibitory peptide of Ca2+/calmodulin dependent protein kinase II (CaM kinase), or a constitutively activated CaM kinase, show altered neuronal process morphology compared to wild type in scanning electron microscopy (SEM) of cultured mature neurons from embryonic neuroblasts. We observed significantly enhanced process growth in cells with inhibited enzyme, and reduced process growth in cells with activated enzyme, suggesting that active CaM kinase is involved in the inhibition of neurite growth during development. The subcellular distribution of CaM kinase in wild type neuronal cultures was determined using a gold particle labeling procedure which allowed the mapping of the enzyme directly in the scanning electron microscope (SEM). Before neuronal contact there was little labeling of processes, but after connections had been made the processes were heavily labeled. Our results suggest that the major transport of CaM kinase to the terminals does not occur until after or during the formation of neuronal connections when a functional synapse might be formed. Taken together, these results suggest a target-dependent transport of the enzyme along processes and an inhibitory role for CaM kinase on neurite branching.",
keywords = "Animals, Biological Transport, Active, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Calcium-Calmodulin-Dependent Protein Kinases, Cells, Cultured, Down-Regulation, Drosophila melanogaster, Genotype, Microscopy, Electron, Scanning, Neurons, Subcellular Fractions, Up-Regulation",
author = "Broughton, {S J} and Kane, {N S} and M Yoder and Greenspan, {R J} and A Robichon",
year = "1996",
month = sep,
day = "15",
doi = "10.1002/(SICI)1097-4644(19960915)62:4<484::AID-JCB6>3.0.CO;2-I",
language = "English",
volume = "62",
pages = "484--494",
journal = "Journal of Cellular Biochemistry",
issn = "0730-2312",
publisher = "Wiley-Liss Inc.",
number = "4",

}

RIS

TY - JOUR

T1 - Transport of CaM kinase along processes elicited by neuronal contact evokes an inhibition of arborization and outgrowth in D. melanogaster cultured neurons

AU - Broughton, S J

AU - Kane, N S

AU - Yoder, M

AU - Greenspan, R J

AU - Robichon, A

PY - 1996/9/15

Y1 - 1996/9/15

N2 - Transgenic Drosophila strains expressing an inhibitory peptide of Ca2+/calmodulin dependent protein kinase II (CaM kinase), or a constitutively activated CaM kinase, show altered neuronal process morphology compared to wild type in scanning electron microscopy (SEM) of cultured mature neurons from embryonic neuroblasts. We observed significantly enhanced process growth in cells with inhibited enzyme, and reduced process growth in cells with activated enzyme, suggesting that active CaM kinase is involved in the inhibition of neurite growth during development. The subcellular distribution of CaM kinase in wild type neuronal cultures was determined using a gold particle labeling procedure which allowed the mapping of the enzyme directly in the scanning electron microscope (SEM). Before neuronal contact there was little labeling of processes, but after connections had been made the processes were heavily labeled. Our results suggest that the major transport of CaM kinase to the terminals does not occur until after or during the formation of neuronal connections when a functional synapse might be formed. Taken together, these results suggest a target-dependent transport of the enzyme along processes and an inhibitory role for CaM kinase on neurite branching.

AB - Transgenic Drosophila strains expressing an inhibitory peptide of Ca2+/calmodulin dependent protein kinase II (CaM kinase), or a constitutively activated CaM kinase, show altered neuronal process morphology compared to wild type in scanning electron microscopy (SEM) of cultured mature neurons from embryonic neuroblasts. We observed significantly enhanced process growth in cells with inhibited enzyme, and reduced process growth in cells with activated enzyme, suggesting that active CaM kinase is involved in the inhibition of neurite growth during development. The subcellular distribution of CaM kinase in wild type neuronal cultures was determined using a gold particle labeling procedure which allowed the mapping of the enzyme directly in the scanning electron microscope (SEM). Before neuronal contact there was little labeling of processes, but after connections had been made the processes were heavily labeled. Our results suggest that the major transport of CaM kinase to the terminals does not occur until after or during the formation of neuronal connections when a functional synapse might be formed. Taken together, these results suggest a target-dependent transport of the enzyme along processes and an inhibitory role for CaM kinase on neurite branching.

KW - Animals

KW - Biological Transport, Active

KW - Calcium-Calmodulin-Dependent Protein Kinase Type 2

KW - Calcium-Calmodulin-Dependent Protein Kinases

KW - Cells, Cultured

KW - Down-Regulation

KW - Drosophila melanogaster

KW - Genotype

KW - Microscopy, Electron, Scanning

KW - Neurons

KW - Subcellular Fractions

KW - Up-Regulation

U2 - 10.1002/(SICI)1097-4644(19960915)62:4<484::AID-JCB6>3.0.CO;2-I

DO - 10.1002/(SICI)1097-4644(19960915)62:4<484::AID-JCB6>3.0.CO;2-I

M3 - Journal article

C2 - 8891894

VL - 62

SP - 484

EP - 494

JO - Journal of Cellular Biochemistry

JF - Journal of Cellular Biochemistry

SN - 0730-2312

IS - 4

ER -