PMID- 10051666
OWN - NLM
STAT- MEDLINE
DCOM- 19990415
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 5
DP  - 1999 Mar 2
TI  - Molecular identification of human G-substrate, a possible downstream component of
      the cGMP-dependent protein kinase cascade in cerebellar Purkinje cells.
PG  - 2467-72
AB  - G-substrate, an endogenous substrate for cGMP-dependent protein kinase, exists
      almost exclusively in cerebellar Purkinje cells, where it is possibly involved in
      the induction of long-term depression. A G-substrate cDNA was identified by
      screening expressed sequence tag databases from a human brain library. The
      deduced amino acid sequence of human G-substrate contained two putative
      phosphorylation sites (Thr-68 and Thr-119) with amino acid sequences
      [KPRRKDT(p)PALH] that were identical to those reported for rabbit G-substrate.
      G-substrate mRNA was expressed almost exclusively in the cerebellum as a single
      transcript. The human G-substrate gene was mapped to human chromosome 7p15 by
      radiation hybrid panel analysis. In vitro translation products of the cDNA showed
      an apparent molecular mass of 24 kDa on SDS/PAGE which was close to that of
      purified rabbit G-substrate (23 kDa). Bacterially expressed human G-substrate is 
      a heat-stable and acid-soluble protein that cross-reacts with antibodies raised
      against rabbit G-substrate. Recombinant human G-substrate was phosphorylated
      efficiently by cGMP-dependent protein kinase exclusively at Thr residues, and it 
      was recognized by antibodies specific for rabbit phospho-G-substrate. The amino
      acid sequences surrounding the sites of phosphorylation in G-substrate are
      related to those around Thr-34 and Thr-35 of the dopamine- and cAMP-regulated
      phosphoprotein DARPP-32 and inhibitor-1, respectively, two potent inhibitors of
      protein phosphatase 1. However, purified G-substrate phosphorylated by
      cGMP-dependent protein kinase inhibited protein phosphatase 2A more effectively
      than protein phosphatase 1, suggesting a distinct role as a protein phosphatase
      inhibitor.
FAU - Endo, S
AU  - Endo S
AD  - Laboratory for Learning and Memory, RIKEN, Brain Science Institute, Hirosawa 2-1,
      Wako, 351-0198, Japan.
FAU - Suzuki, M
AU  - Suzuki M
FAU - Sumi, M
AU  - Sumi M
FAU - Nairn, A C
AU  - Nairn AC
FAU - Morita, R
AU  - Morita R
FAU - Yamakawa, K
AU  - Yamakawa K
FAU - Greengard, P
AU  - Greengard P
FAU - Ito, M
AU  - Ito M
LA  - eng
SI  - GENBANK/AF097730
GR  - P01 DA010044/DA/NIDA NIH HHS/United States
GR  - P01 MH040899/MH/NIMH NIH HHS/United States
GR  - DA-10044/DA/NIDA NIH HHS/United States
GR  - MH-40899/MH/NIMH NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (G-substrate)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (Recombinant Proteins)
RN  - EC 2.7.11.12 (Cyclic GMP-Dependent Protein Kinases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Brain/*metabolism
MH  - Cerebellum/*physiology
MH  - Cloning, Molecular
MH  - Cyclic GMP-Dependent Protein Kinases/*metabolism
MH  - Databases as Topic
MH  - Expressed Sequence Tags
MH  - Humans
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/chemistry/*genetics/*metabolism
MH  - Purkinje Cells/*physiology
MH  - RNA, Messenger/analysis
MH  - Rabbits
MH  - Recombinant Proteins/biosynthesis/chemistry
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Transcription, Genetic
PMC - PMC26808
EDAT- 1999/03/03 00:00
MHDA- 1999/03/03 00:01
CRDT- 1999/03/03 00:00
PHST- 1999/03/03 00:00 [pubmed]
PHST- 1999/03/03 00:01 [medline]
PHST- 1999/03/03 00:00 [entrez]
AID - 10.1073/pnas.96.5.2467 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2467-72. doi: 10.1073/pnas.96.5.2467.