PMID- 10403843
OWN - NLM
STAT- MEDLINE
DCOM- 19990816
LR  - 20161122
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 260
IP  - 3
DP  - 1999 Jul 14
TI  - DNA binding activity of the fetal Alz-50 clone 1 (FAC1) protein is enhanced by
      phosphorylation.
PG  - 785-9
AB  - Fetal Alz-50 clone 1 (FAC1) is a novel DNA binding protein with altered
      expression and subcellular localization during neuronal development and
      degeneration. FAC1 localizes to the cell body and neurites in undifferentiated
      neurons during development and in degenerating neurons during Alzheimer's disease
      progression. In the normal adult brain FAC1 is present predominantly in the
      nucleus of cortical neurons. When in the nucleus FAC1 has been shown to repress
      transcription by binding a specific DNA sequence. In the present study we
      demonstrate that the affinity of FAC1 for the identified DNA sequence is
      dramatically enhanced when FAC1 is phosphorylated. Phosphatase treatment of
      neuroblastoma nuclear extracts reduces FAC1 DNA binding affinity. Finally,
      inhibition of cellular serine/threonine phosphatases results in increased FAC1
      DNA binding activity. These data suggest that FAC1 DNA binding activity is
      dependent upon and regulated by phosphorylation signals in the cell.
CI  - Copyright 1999 Academic Press.
FAU - Jordan-Sciutto, K L
AU  - Jordan-Sciutto KL
AD  - Department of Pathology, University of Pittsburgh School of Medicine, Pittsburgh,
      Pennsylvania, 15261, USA.
FAU - Dragich, J M
AU  - Dragich JM
FAU - Bowser, R
AU  - Bowser R
LA  - eng
GR  - AG13208/AG/NIA NIH HHS/United States
GR  - AG05133/AG/NIA NIH HHS/United States
GR  - NS10572/NS/NINDS NIH HHS/United States
GR  - F32 NS010572-02/NS/NINDS NIH HHS/United States
GR  - F32 NS010572/NS/NINDS NIH HHS/United States
GR  - F32 NS010572-01/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Antigens, Nuclear)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Transcription Factors)
RN  - 0 (fetal Alzheimer antigen)
RN  - 1W21G5Q4N2 (Okadaic Acid)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - 9007-49-2 (DNA)
RN  - EC 3.1.3.16 (Phosphoprotein Phosphatases)
RN  - EC 3.1.3.2 (Acid Phosphatase)
SB  - IM
MH  - Acid Phosphatase/metabolism
MH  - Adenosine Triphosphate/metabolism
MH  - Animals
MH  - Antigens, Nuclear
MH  - Cell Nucleus/metabolism
MH  - DNA/genetics/*metabolism
MH  - DNA-Binding Proteins/isolation & purification/*metabolism
MH  - Humans
MH  - Nerve Tissue Proteins/isolation & purification/*metabolism
MH  - Neuroblastoma
MH  - Neurons/*metabolism
MH  - Nuclear Proteins/metabolism
MH  - Okadaic Acid/pharmacology
MH  - PC12 Cells
MH  - Phosphoprotein Phosphatases/antagonists & inhibitors/metabolism
MH  - Phosphorylation
MH  - Protein Binding
MH  - Rats
MH  - Recombinant Fusion Proteins/isolation & purification/metabolism
MH  - Response Elements/genetics
MH  - *Transcription Factors
MH  - Tumor Cells, Cultured
EDAT- 1999/07/15 00:00
MHDA- 1999/07/15 00:01
CRDT- 1999/07/15 00:00
PHST- 1999/07/15 00:00 [pubmed]
PHST- 1999/07/15 00:01 [medline]
PHST- 1999/07/15 00:00 [entrez]
AID - 10.1006/bbrc.1999.0986 [doi]
AID - S0006-291X(99)90986-5 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1999 Jul 14;260(3):785-9. doi:
      10.1006/bbrc.1999.0986.