PMID- 10504266
OWN - NLM
STAT- MEDLINE
DCOM- 19991020
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 38
IP  - 39
DP  - 1999 Sep 28
TI  - Regulation of neurabin I interaction with protein phosphatase 1 by
      phosphorylation.
PG  - 12943-9
AB  - Neurabin I is a brain-specific actin-binding protein. Here we show that neurabin 
      I binds protein phosphatase 1 (PP1) and inhibits PP1 activity. Neurabin I
      interacted with PP1alpha in an overlay assay, in yeast two-hybrid interaction
      analysis, and in coprecipitation and co-immunoprecipitation experiments. Neurabin
      I also copurified with both the alpha and gamma isoforms of PP1. A glutathione
      S-transferase (GST)-neurabin I fusion protein (residues 318-661) containing the
      putative PP1 binding domain (residues 456-460) inhibited PP1 activity (K(i) = 2.7
      +/- 1.2 nM). This fusion protein was also rapidly phosphorylated in vitro by PKA 
      (K(m) = 6 microM) to a stoichiomtry of 1 mol/mol. The phosphorylated residue was 
      identified as serine 461 by HPLC-MS analysis of a tryptic digest. Phosphorylation
      of GST-neurabin I (residues 318-661) by PKA significantly reduced its binding to 
      PP1 by overlay and by glutathione-Sepharose coprecipitation assays. A 35-fold
      decrease in inhibitory potency was also observed using a S461E mutant, which
      mimics phosphorylation of S461. These findings identify a signaling mechanism
      involving the regulation of PP1 activity and localization mediated by the cAMP
      pathway.
FAU - McAvoy, T
AU  - McAvoy T
AD  - Departments of Anesthesiology and Pharmacology, Weill Medical College of Cornell 
      University, New York, New York 10021, USA.
FAU - Allen, P B
AU  - Allen PB
FAU - Obaishi, H
AU  - Obaishi H
FAU - Nakanishi, H
AU  - Nakanishi H
FAU - Takai, Y
AU  - Takai Y
FAU - Greengard, P
AU  - Greengard P
FAU - Nairn, A C
AU  - Nairn AC
FAU - Hemmings, H C Jr
AU  - Hemmings HC Jr
LA  - eng
GR  - P01 DA010044/DA/NIDA NIH HHS/United States
GR  - DA10044/DA/NIDA NIH HHS/United States
GR  - MH40899/MH/NIMH NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Microfilament Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (neurabin)
RN  - EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases)
RN  - EC 3.1.3.16 (Phosphoprotein Phosphatases)
RN  - EC 3.1.3.16 (Protein Phosphatase 1)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Brain/enzymology/metabolism
MH  - Cyclic AMP-Dependent Protein Kinases/metabolism
MH  - Male
MH  - Microfilament Proteins/*metabolism
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/*metabolism
MH  - Peptide Fragments/chemistry
MH  - Phosphoprotein Phosphatases/chemistry/*metabolism
MH  - Phosphorylation
MH  - Precipitin Tests
MH  - Protein Phosphatase 1
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Sequence Homology, Amino Acid
EDAT- 1999/10/03 09:00
MHDA- 2001/03/28 10:01
CRDT- 1999/10/03 09:00
PHST- 1999/10/03 09:00 [pubmed]
PHST- 2001/03/28 10:01 [medline]
PHST- 1999/10/03 09:00 [entrez]
AID - bi991227d [pii]
AID - 10.1021/bi991227d [doi]
PST - ppublish
SO  - Biochemistry. 1999 Sep 28;38(39):12943-9. doi: 10.1021/bi991227d.