PMID- 7760048
OWN - NLM
STAT- MEDLINE
DCOM- 19950628
LR  - 20211203
IS  - 0022-3042 (Print)
IS  - 0022-3042 (Linking)
VI  - 64
IP  - 6
DP  - 1995 Jun
TI  - Neuronal cyclin-dependent kinase-5 phosphorylation sites in neurofilament protein 
      (NF-H) are dephosphorylated by protein phosphatase 2A.
PG  - 2681-90
AB  - Neurofilament (NF) protein [high molecular mass (NF-H)] is extensively 
      phosphorylated in vivo. The phosphorylation occurs mainly in its characteristic 
      KSP (Lys-Ser-Pro) repeat motifs. There are two major types of KSP motifs in the 
      NF-H tail domain: KSPXKX and KSPXXX. Recent studies by two different laboratories 
      have demonstrated the presence of a cdc2-like kinase [cyclin-dependent kinase-5 
      (cdk5)] in nervous tissue that selectively phosphorylates KSPXKX and XS/TXK 
      motifs in NF-H and lysine-rich histone (H1). This article describes the 
      identification of phosphatases dephosphorylating three different substrates: 
      histone (H1), NF-H in a NF preparation, and a bacterially expressed C-terminal 
      tail domain of NF-H, each containing KSPXKX repeats phosphorylated in vitro by 
      cdk5. Among various phosphatases identified, protein phosphatase (PP) 2A from 
      rabbit skeletal muscle appeared to be the most effective phosphatase in in vitro 
      assays. Three phosphatase activity peaks--P1, P2, and P3--were partially purified 
      from frozen rat spinal cord by ion exchange and size exclusion column 
      chromatography and then characterized on the basis of biochemical, 
      pharmacological, and immunochemical studies. One of the three peaks was 
      identified as PP2A, whereas the others were mixtures of both PP2A and PP1. These 
      three peaks could dephosphorylate cdk5-phosphorylated 32P-histone (H1), 32P-NF-H 
      in the NF preparation, and 32P-NF-H tail fusion protein. These studies suggest 
      the involvement of PP2A or a PP2A-like activity in the regulation of the 
      phosphorylation state of KSPXKX motifs in NF-H.
FAU - Veeranna
AU  - Veeranna
AD  - Laboratory of Neurochemistry, National Institute of Neurological Disorders and 
      Stroke, National Institutes of Health, Bethesda, MD 20892, USA.
FAU - Shetty, K T
AU  - Shetty KT
FAU - Link, W T
AU  - Link WT
FAU - Jaffe, H
AU  - Jaffe H
FAU - Wang, J
AU  - Wang J
FAU - Pant, H C
AU  - Pant HC
LA  - eng
PT  - Journal Article
PL  - England
TA  - J Neurochem
JT  - Journal of neurochemistry
JID - 2985190R
RN  - 0 (Ethers, Cyclic)
RN  - 0 (Histones)
RN  - 0 (Microcystins)
RN  - 0 (Neurofilament Proteins)
RN  - 0 (Peptides, Cyclic)
RN  - 108688-71-7 (neurofilament protein H)
RN  - 1W21G5Q4N2 (Okadaic Acid)
RN  - 77238-39-2 (microcystin)
RN  - EC 2.7.11.1 (Cyclin-Dependent Kinase 5)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
RN  - EC 2.7.11.22 (Cdk5 protein, rat)
RN  - EC 2.7.11.22 (Cyclin-Dependent Kinases)
RN  - EC 3.1.3.16 (Phosphoprotein Phosphatases)
RN  - EC 3.1.3.16 (Protein Phosphatase 2)
RN  - EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
SB  - IM
MH  - Animals
MH  - Cyclin-Dependent Kinase 5
MH  - *Cyclin-Dependent Kinases
MH  - Ethers, Cyclic/pharmacology
MH  - Histones/metabolism
MH  - Microcystins
MH  - Neurofilament Proteins/genetics/*metabolism
MH  - Neurons/*enzymology
MH  - Okadaic Acid
MH  - Peptides, Cyclic/pharmacology
MH  - Phosphoprotein Phosphatases/antagonists & inhibitors/*metabolism
MH  - Phosphoric Monoester Hydrolases/metabolism
MH  - Phosphorylation
MH  - Protein Phosphatase 2
MH  - Protein Serine-Threonine Kinases/*metabolism
MH  - Rats
MH  - Repetitive Sequences, Nucleic Acid
MH  - Spinal Cord/enzymology
EDAT- 1995/06/01 00:00
MHDA- 1995/06/01 00:01
CRDT- 1995/06/01 00:00
PHST- 1995/06/01 00:00 [pubmed]
PHST- 1995/06/01 00:01 [medline]
PHST- 1995/06/01 00:00 [entrez]
AID - 10.1046/j.1471-4159.1995.64062681.x [doi]
PST - ppublish
SO  - J Neurochem. 1995 Jun;64(6):2681-90. doi: 10.1046/j.1471-4159.1995.64062681.x.