The molecular features in PKC epsilon determining its neurite-inducing capacity
(2005)- Abstract
- Protein kinase C (PKC) is a family of serine/threonine kinases which are subgrouped into classical (a, bI, bII, g), novel (d, e, h, q) and atypical (z, i/l) isoforms.
It has been shown that PKCe induces neurite outgrowth in neuroblastoma cells and the effect is mediated via the regulatory domain. One aim of this study was to identify the structures in PKCe that mediate neurite outgrowth. This study shows that PKCe-induced neurite outgrowth can be obtained in several other neural cell lines and that PKC catalytic activity and the RhoA pathway can counteract neurite outgrowth. A region of PKCe encompassing the two C1 domains and flanking residues was shown to be sufficient for neurite induction. The corresponding region... (More) - Protein kinase C (PKC) is a family of serine/threonine kinases which are subgrouped into classical (a, bI, bII, g), novel (d, e, h, q) and atypical (z, i/l) isoforms.
It has been shown that PKCe induces neurite outgrowth in neuroblastoma cells and the effect is mediated via the regulatory domain. One aim of this study was to identify the structures in PKCe that mediate neurite outgrowth. This study shows that PKCe-induced neurite outgrowth can be obtained in several other neural cell lines and that PKC catalytic activity and the RhoA pathway can counteract neurite outgrowth. A region of PKCe encompassing the two C1 domains and flanking residues was shown to be sufficient for neurite induction. The corresponding region from all novel PKC isoforms, but not PKCa, had neurite-inducing capacity. Furthermore, a conserved motif immediately N-terminal of the PKCe C1b domain, was found to be required for neurite induction, and specifically, mutation of either Phe-237, Val-239 or Met-241 within this motif abolished neurite outgrowth. The isolated PKCe C1b domain including twelve N-terminal and twenty C-terminal residues could induce neurite outgrowth in the presence of phorbol ester. It was also shown that specific structures in the PKCe C1b domain are required for neurite induction. Residues in the C-terminal end of the PKCe C1b domain localised at the base of the globular C1 domain, in the proximity of the motif N-terminal of the C1b domain, were identified as important for neurite outgrowth. Thus individual residues determining isoform-specific effects of PKC have been identified. (Less)
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https://lup.lub.lu.se/record/545911
- author
- Ling, Mia LU
- supervisor
- opponent
-
- Dr Hall, Christine, Inst of Neurology, University College London, UK
- organization
- publishing date
- 2005
- type
- Thesis
- publication status
- published
- subject
- keywords
- oncology, Cytology, neuroblastoma, neurite outgrowth, C1 domain, cancerology, cancer, onkologi, Cytologi, protein kinase C
- pages
- 95 pages
- publisher
- Division of Molecular Medicine, Department of Laboratory Medicine, UMAS, Malmö
- defense location
- Föreläsningssalen, Patologihuset, Universitetssjukhuset MAS, Malmö.
- defense date
- 2005-12-16 09:15:00
- ISBN
- 91-85481-22-x
- language
- English
- LU publication?
- yes
- additional info
- Mia Ling. 2004. Induction of neurites by the regulatory domains of PKC? and ? is counteracted by PKC catalytic activity and by the RhoA pathway. Exp Cell Res., vol 292 pp 135-150.Mia Ling, Ulrika Trollér, Ruth Zeidman, Cecilia Lundberg and Christer Larsson. 2004. Induction of neurites by the regulatory domains of PKC? and ? is counteracted by PKC catalytic activity and by the RhoA pathway. Exp Cell Res., vol 292 pp 135-150.Mia Ling, Ulrika Trollér, Ruth Zeidman, Helena Stensman, Anna Schultz and Christer Larsson. 2005. Identifi cation of conserved amino acids N-terminal of the PKC? C1b domain crucial for PKC?-mediated neurite outgrowth. J Biol Chem, vol 280 pp 17910-17919.Mia Ling and Christer Larsson. . Comparison of the PKC? and PKC? C1b domains: Identifi cation of residues critical for PKC?-mediated neurite induction. (manuscript)The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Molecular Medicine (013031200)
- id
- e2fd2695-712d-4101-b264-f403edd970c9 (old id 545911)
- date added to LUP
- 2016-04-01 16:15:53
- date last changed
- 2018-11-21 20:40:02
@phdthesis{e2fd2695-712d-4101-b264-f403edd970c9, abstract = {{Protein kinase C (PKC) is a family of serine/threonine kinases which are subgrouped into classical (a, bI, bII, g), novel (d, e, h, q) and atypical (z, i/l) isoforms.<br/><br> <br/><br> It has been shown that PKCe induces neurite outgrowth in neuroblastoma cells and the effect is mediated via the regulatory domain. One aim of this study was to identify the structures in PKCe that mediate neurite outgrowth. This study shows that PKCe-induced neurite outgrowth can be obtained in several other neural cell lines and that PKC catalytic activity and the RhoA pathway can counteract neurite outgrowth. A region of PKCe encompassing the two C1 domains and flanking residues was shown to be sufficient for neurite induction. The corresponding region from all novel PKC isoforms, but not PKCa, had neurite-inducing capacity. Furthermore, a conserved motif immediately N-terminal of the PKCe C1b domain, was found to be required for neurite induction, and specifically, mutation of either Phe-237, Val-239 or Met-241 within this motif abolished neurite outgrowth. The isolated PKCe C1b domain including twelve N-terminal and twenty C-terminal residues could induce neurite outgrowth in the presence of phorbol ester. It was also shown that specific structures in the PKCe C1b domain are required for neurite induction. Residues in the C-terminal end of the PKCe C1b domain localised at the base of the globular C1 domain, in the proximity of the motif N-terminal of the C1b domain, were identified as important for neurite outgrowth. Thus individual residues determining isoform-specific effects of PKC have been identified.}}, author = {{Ling, Mia}}, isbn = {{91-85481-22-x}}, keywords = {{oncology; Cytology; neuroblastoma; neurite outgrowth; C1 domain; cancerology; cancer; onkologi; Cytologi; protein kinase C}}, language = {{eng}}, publisher = {{Division of Molecular Medicine, Department of Laboratory Medicine, UMAS, Malmö}}, school = {{Lund University}}, title = {{The molecular features in PKC epsilon determining its neurite-inducing capacity}}, year = {{2005}}, }