PMID- 23600483
OWN - NLM
STAT- MEDLINE
DCOM- 20141009
LR  - 20191210
IS  - 1365-2443 (Electronic)
IS  - 1356-9597 (Linking)
VI  - 18
IP  - 7
DP  - 2013 Jul
TI  - CaMKIIbeta-mediated LIM-kinase activation plays a crucial role in BDNF-induced 
      neuritogenesis.
PG  - 533-43
LID - 10.1111/gtc.12054 [doi]
AB  - LIM-kinase 1 (LIMK1) regulates actin cytoskeletal reorganization by 
      phosphorylating and inactivating actin-depolymerizing factor and cofilin. We 
      examined the role of LIMK1 in brain-derived neurotrophic factor (BDNF)-induced 
      neuritogenesis in primary-cultured rat cortical neurons. Knockdown of LIMK1 or 
      expression of a kinase-dead LIMK1 mutant suppressed BDNF-induced enhancement of 
      primary neurite formation. By contrast, expression of an active form of LIMK1 
      promoted primary neuritogenesis in the absence of BDNF. BDNF-induced 
      neuritogenesis was inhibited by KN-93, an inhibitor of Ca(2+) 
      /calmodulin-dependent protein kinases (CaMKs), but not by STO-609, an inhibitor 
      of CaMK-kinase (CaMKK). CaMKK activity is required for the activation of CaMKI 
      and CaMKIV, but not CaMKII, which suggests that CaMKII is principally involved in 
      BDNF-induced enhancement of neuritogenesis. Knockdown of CaMKIIbeta, but not 
      CaMKIIalpha, suppressed BDNF-induced neuritogenesis. Active CaMKIIbeta promoted 
      neuritogenesis, and this promotion was inhibited by knockdown of LIMK1, 
      indicating that CaMKIIbeta is involved in BDNF-induced neuritogenesis via activation 
      of LIMK1. Furthermore, in vitro kinase assays revealed that CaMKIIbeta 
      phosphorylates LIMK1 at Thr-508 in the kinase domain and activates the 
      cofilin-phosphorylating activity of LIMK1. In summary, these results suggest that 
      CaMKIIbeta-mediated activation of LIMK1 plays a crucial role in BDNF-induced 
      enhancement of primary neurite formation.
CI  - (c) 2013 The Authors Genes to Cells (c) 2013 by the Molecular Biology Society of 
      Japan and Wiley Publishing Asia Pty Ltd.
FAU - Saito, Akihiko
AU  - Saito A
AD  - Department of Biomolecular Sciences, Graduate School of Life Sciences, Tohoku 
      University, Sendai, Miyagi, 980-8578, Japan.
FAU - Miyajima, Ken
AU  - Miyajima K
FAU - Akatsuka, Junichi
AU  - Akatsuka J
FAU - Kondo, Hiroshi
AU  - Kondo H
FAU - Mashiko, Toshiya
AU  - Mashiko T
FAU - Kiuchi, Tai
AU  - Kiuchi T
FAU - Ohashi, Kazumasa
AU  - Ohashi K
FAU - Mizuno, Kensaku
AU  - Mizuno K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130418
PL  - England
TA  - Genes Cells
JT  - Genes to cells : devoted to molecular & cellular mechanisms
JID - 9607379
RN  - 0 (Benzylamines)
RN  - 0 (Brain-Derived Neurotrophic Factor)
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Camk2n1 protein, rat)
RN  - 0 (Carrier Proteins)
RN  - 0 (Sulfonamides)
RN  - 139298-40-1 (KN 93)
RN  - 7171WSG8A2 (BDNF protein, human)
RN  - EC 2.7.11.1 (Lim Kinases)
RN  - EC 2.7.11.1 (Limk1 protein, rat)
SB  - IM
MH  - Animals
MH  - Benzylamines/pharmacology
MH  - Brain-Derived Neurotrophic Factor/antagonists & inhibitors/*metabolism
MH  - Calcium-Binding Proteins
MH  - Carrier Proteins/*metabolism
MH  - Cells, Cultured
MH  - Lim Kinases/*metabolism
MH  - Neurites/*metabolism
MH  - *Neurogenesis
MH  - Neurons/metabolism
MH  - Phosphorylation
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Structure-Activity Relationship
MH  - Sulfonamides/pharmacology
EDAT- 2013/04/23 06:00
MHDA- 2014/10/10 06:00
CRDT- 2013/04/23 06:00
PHST- 2013/03/10 00:00 [accepted]
PHST- 2013/03/04 00:00 [received]
PHST- 2013/04/23 06:00 [entrez]
PHST- 2013/04/23 06:00 [pubmed]
PHST- 2014/10/10 06:00 [medline]
AID - 10.1111/gtc.12054 [doi]
PST - ppublish
SO  - Genes Cells. 2013 Jul;18(7):533-43. doi: 10.1111/gtc.12054. Epub 2013 Apr 18.