PMID- 10593988
OWN - NLM
STAT- MEDLINE
DCOM- 20000127
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 51
DP  - 1999 Dec 17
TI  - Novel inositol polyphosphate 5-phosphatase localizes at membrane ruffles.
PG  - 36790-5
AB  - We have cloned a novel inositol polyphosphate 5-phosphatase from the rat brain
      cDNA library. It contains two highly conserved 5-phosphatase motifs, both of
      which are essential for its enzymatic activity. Interestingly, the proline
      content of this protein is high and concentrated in its N- and C-terminal
      regions. One putative SH3-binding motif and six 14-3-3 zeta-binding motifs were
      found in the amino acid sequence. This enzyme hydrolyzed phosphate at the D-5
      position of inositol 1,4,5-trisphosphate, inositol 1,3,4, 5-tetrakisphosphate,
      and phosphatidylinositol 4,5-bisphosphate, consistent with the substrate
      specificity of type II 5-phosphatase, OCRL, synaptojanin and synaptojanin 2,
      already characterized 5-phosphatases. When the Myc-epitope-tagged enzyme was
      expressed in COS-7 cells and stained with anti-Myc polyclonal antibody, a signal 
      was observed at ruffling membranes and in the cytoplasm. We prepared several
      deletion mutants and demonstrated that the 123 N-terminal amino acids (311-433)
      and a C-terminal proline-rich region containing 277 amino acids (725-1001) were
      essential for its localization to ruffling membranes. This enzyme might regulate 
      the level of inositol and phosphatidylinositol polyphosphates at membrane
      ruffles.
FAU - Mochizuki, Y
AU  - Mochizuki Y
AD  - Department of Biochemistry, The Institute of Medical Science, University of
      Tokyo, Minato-ku, Tokyo 108-8639, Japan.
FAU - Takenawa, T
AU  - Takenawa T
LA  - eng
SI  - GENBANK/AB032551
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Membrane Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
RN  - EC 3.1.3.56 (Inositol Polyphosphate 5-Phosphatases)
SB  - IM
EIN - J Biol Chem 2000 Jul 7;275(27):20956
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Brain/enzymology
MH  - COS Cells
MH  - Cell Membrane/*enzymology
MH  - Cloning, Molecular
MH  - Inositol Polyphosphate 5-Phosphatases
MH  - Membrane Proteins/*genetics/metabolism
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/genetics/metabolism
MH  - Phosphoric Monoester Hydrolases/*genetics/isolation & purification/metabolism
MH  - Rats
MH  - Sequence Alignment
EDAT- 1999/12/14 00:00
MHDA- 1999/12/14 00:01
CRDT- 1999/12/14 00:00
PHST- 1999/12/14 00:00 [pubmed]
PHST- 1999/12/14 00:01 [medline]
PHST- 1999/12/14 00:00 [entrez]
AID - 10.1074/jbc.274.51.36790 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Dec 17;274(51):36790-5. doi: 10.1074/jbc.274.51.36790.