PMID- 23420842
OWN - NLM
STAT- MEDLINE
DCOM- 20130530
LR  - 20211021
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 288
IP  - 13
DP  - 2013 Mar 29
TI  - Casein kinase 2 phosphorylation of protein kinase C and casein kinase 2 substrate 
      in neurons (PACSIN) 1 protein regulates neuronal spine formation.
PG  - 9303-12
LID - 10.1074/jbc.M113.461293 [doi]
AB  - The PACSIN (protein kinase C and casein kinase 2 substrate in neurons) adapter 
      proteins couple components of the clathrin-mediated endocytosis machinery with 
      regulators of actin polymerization and thereby regulate the surface expression of 
      specific receptors. The brain-specific PACSIN 1 is enriched at synapses and has 
      been proposed to affect neuromorphogenesis and the formation and maturation of 
      dendritic spines. In studies of how phosphorylation of PACSIN 1 contributes to 
      neuronal function, we identified serine 358 as a specific site used by casein 
      kinase 2 (CK2) in vitro and in vivo. Phosphorylated PACSIN 1 was found in 
      neuronal cytosol and membrane fractions. This localization could be modulated by 
      trophic factors such as brain-derived neurotrophic factor (BDNF). We further show 
      that expression of a phospho-negative PACSIN 1 mutant, S358A, or inhibition of 
      CK2 drastically reduces spine formation in neurons. We identified a novel protein 
      complex containing the spine regulator Rac1, its GTPase-activating protein 
      neuron-associated developmentally regulated protein (NADRIN), and PACSIN 1. CK2 
      phosphorylation of PACSIN 1 leads to a dissociation of the complex upon BDNF 
      treatment and induces Rac1-dependent spine formation in dendrites of hippocampal 
      neurons. These findings suggest that upon BDNF signaling PACSIN 1 is 
      phosphorylated by CK2 which is essential for spine formation.
FAU - Schael, Sylvia
AU  - Schael S
AD  - Center for Biochemistry, University of Cologne, D-50931, Cologne, Germany.
FAU - Nuchel, Julian
AU  - Nuchel J
FAU - Muller, Stefan
AU  - Muller S
FAU - Petermann, Philipp
AU  - Petermann P
FAU - Kormann, Jan
AU  - Kormann J
FAU - Perez-Otano, Isabel
AU  - Perez-Otano I
FAU - Martinez, Sonia Marco
AU  - Martinez SM
FAU - Paulsson, Mats
AU  - Paulsson M
FAU - Plomann, Markus
AU  - Plomann M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130218
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Clathrin)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Neuropeptides)
RN  - 0 (Pacsin1 protein, mouse)
RN  - 0 (Phosphoproteins)
RN  - 452VLY9402 (Serine)
RN  - EC 2.7.11.1 (Casein Kinase II)
RN  - EC 2.7.11.13 (Protein Kinase C)
RN  - EC 3.6.5.2 (rac1 GTP-Binding Protein)
SB  - IM
MH  - Adaptor Proteins, Signal Transducing
MH  - Animals
MH  - Brain/metabolism
MH  - Casein Kinase II/*metabolism
MH  - Clathrin/metabolism
MH  - Dendrites
MH  - Gene Silencing
MH  - Intracellular Signaling Peptides and Proteins
MH  - Mice
MH  - Microscopy, Fluorescence/methods
MH  - Models, Biological
MH  - Mutation
MH  - Neuronal Plasticity
MH  - Neurons/metabolism
MH  - Neuropeptides/*metabolism
MH  - Phosphoproteins/*metabolism
MH  - Phosphorylation
MH  - Protein Kinase C/*metabolism
MH  - Serine/metabolism
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH  - Synapses/metabolism
MH  - Synaptic Transmission
MH  - rac1 GTP-Binding Protein/*metabolism
PMC - PMC3611001
EDAT- 2013/02/20 06:00
MHDA- 2013/06/01 06:00
PMCR- 2014/03/29
CRDT- 2013/02/20 06:00
PHST- 2013/02/20 06:00 [entrez]
PHST- 2013/02/20 06:00 [pubmed]
PHST- 2013/06/01 06:00 [medline]
PHST- 2014/03/29 00:00 [pmc-release]
AID - S0021-9258(19)35089-6 [pii]
AID - M113.461293 [pii]
AID - 10.1074/jbc.M113.461293 [doi]
PST - ppublish
SO  - J Biol Chem. 2013 Mar 29;288(13):9303-12. doi: 10.1074/jbc.M113.461293. Epub 2013 
      Feb 18.