Inhibition of neurite extension by overexpression of individual domains of LIM kinase 1

Lin‐11, Isl‐1 and Mec‐3 (LIM) kinases are serine/threonine kinases that phosphorylate cofilin, an actin depolymerizing protein. LIM kinases have a highly modular structure composed of two N‐terminal LIM domains (LIM 1/2), a PSD‐95, Dlg and ZO‐1 (PDZ) domain and a C‐terminal protein kinase domain. He...

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Published inJournal of neurochemistry Vol. 78; no. 4; pp. 924 - 927
Main Authors Birkenfeld, Jörg, Betz, Heinrich, Roth, Dagmar
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Science Ltd 01.08.2001
Blackwell
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Abstract Lin‐11, Isl‐1 and Mec‐3 (LIM) kinases are serine/threonine kinases that phosphorylate cofilin, an actin depolymerizing protein. LIM kinases have a highly modular structure composed of two N‐terminal LIM domains (LIM 1/2), a PSD‐95, Dlg and ZO‐1 (PDZ) domain and a C‐terminal protein kinase domain. Here, we overexpressed individual domains of mouse LIM kinase 1 (LIMK1) in PC12 cells and investigated their effects on neurite outgrowth. Although none of the LIMK1 domains had an effect on spontaneous neurite outgrowth, the N‐terminal LIM 1/2 domains strongly inhibited differentiation of PC12 cells after stimulation with both nerve growth factor (NGF) and the Rho‐kinase inhibitor Y‐27632. In contrast, the overexpressed PDZ domain reduced neurite outgrowth only when differentiation had been induced by Y‐27632, but not by NGF. Our data suggest that the different non‐catalytic N‐terminal domains of LIMK1 contribute to the regulation of neurite extension by using distinct signal transduction pathways.
AbstractList Lin-11, Isl-1 and Mec-3 (LIM) kinases are serine/threonine kinases that phosphorylate cofilin, an actin depolymerizing protein. LIM kinases have a highly modular structure composed of two N-terminal LIM domains (LIM 1/2), a PSD-95, Dlg and ZO-1 (PDZ) domain and a C-terminal protein kinase domain. Here, we overexpressed individual domains of mouse LIM kinase 1 (LIMK1) in PC12 cells and investigated their effects on neurite outgrowth. Although none of the LIMK1 domains had an effect on spontaneous neurite outgrowth, the N-terminal LIM 1/2 domains strongly inhibited differentiation of PC12 cells after stimulation with both nerve growth factor (NGF) and the Rho-kinase inhibitor Y-27632. In contrast, the overexpressed PDZ domain reduced neurite outgrowth only when differentiation had been induced by Y-27632, but not by NGF. Our data suggest that the different non-catalytic N-terminal domains of LIMK1 contribute to the regulation of neurite extension by using distinct signal transduction pathways.
Author Betz, Heinrich
Roth, Dagmar
Birkenfeld, Jörg
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  surname: Roth
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Issue 4
Keywords Cell line
Neurite
Enzyme
Growth
Kinase
Transferases
Gene overexpression
Molecular domain
Language English
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  article-title: LIMK‐1 and LIMK‐2, two members of a LIM motif‐containing protein kinase family
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SSID ssj0016461
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Snippet Lin‐11, Isl‐1 and Mec‐3 (LIM) kinases are serine/threonine kinases that phosphorylate cofilin, an actin depolymerizing protein. LIM kinases have a highly...
Lin-11, Isl-1 and Mec-3 (LIM) kinases are serine/threonine kinases that phosphorylate cofilin, an actin depolymerizing protein. LIM kinases have a highly...
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pascalfrancis
wiley
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StartPage 924
SubjectTerms actin
Amides - pharmacology
Animals
Biological and medical sciences
Cell Line
Cell Size
cofilin
Enzyme Inhibitors - pharmacology
Fundamental and applied biological sciences. Psychology
Genes, Reporter
Humans
Immunoblotting
Immunohistochemistry
Isolated neuron and nerve. Neuroglia
LIM kinase 1
Lim Kinases
Mice
Nerve Growth Factor - pharmacology
neurite outgrowth
Neurites - drug effects
Neurites - metabolism
PC12 cells
Protein Kinases - genetics
Protein Kinases - metabolism
Protein Structure, Tertiary
Pyridines - pharmacology
Rats
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Two-Hybrid System Techniques
Vertebrates: nervous system and sense organs
Title Inhibition of neurite extension by overexpression of individual domains of LIM kinase 1
URI https://onlinelibrary.wiley.com/doi/abs/10.1046%2Fj.1471-4159.2001.00500.x
https://www.ncbi.nlm.nih.gov/pubmed/11520913
https://search.proquest.com/docview/18196224
https://search.proquest.com/docview/71119017
Volume 78
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