Pubmed-entry ::= {
pmid 15721295,
medent {
em std {
year 2005,
month 2,
day 21
},
cit {
title {
name "Phosphorylation-dependent binding of 14-3-3 to Par3beta, a human
Par3-related cell polarity protein."
},
authors {
names ml {
"Izaki T",
"Kamakura S",
"Kohjima M",
"Sumimoto H"
},
affil str "Medical Institute of Bioregulation, Kyushu University,
3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan."
},
from journal {
title {
iso-jta "Biochem. Biophys. Res. Commun.",
ml-jta "Biochem Biophys Res Commun",
issn "0006-291X",
name "Biochemical and biophysical research communications"
},
imp {
date std {
year 2005,
month 4,
day 1
},
volume "329",
issue "1",
pages "211-218",
language "eng",
pubstatus ppublish,
history {
{
pubstatus received,
date std {
year 2005,
month 1,
day 18
}
},
{
pubstatus pubmed,
date std {
year 2005,
month 2,
day 22,
hour 9,
minute 0
}
},
{
pubstatus medline,
date std {
year 2005,
month 4,
day 14,
hour 9,
minute 0
}
},
{
pubstatus other,
date std {
year 2005,
month 2,
day 22,
hour 9,
minute 0
}
}
}
}
},
ids {
pii "S0006-291X(05)00181-6",
doi "10.1016/j.bbrc.2005.01.115",
pubmed 15721295
}
},
abstract "Mammalian Par3alpha and Par3beta/Par3L participate in cell
polarity establishment and localize to tight junctions of epithelial cells;
Par3alpha acts via binding to atypical PKC (aPKC). Here we show that Par3beta
as well as Par3alpha interacts with 14-3-3 proteins in a
phosphorylation-dependent manner. In the interaction, Ser-746 of Par3beta and
the corresponding residue of Par3alpha (Ser-814) likely play a crucial role,
since replacement of these residues by unphosphorylatable alanine results in
a loss of interacting activity. The mutant Par3 proteins with the replacement
are correctly recruited to tight junctions of MDCK cells and to membrane
ruffles induced by an active form of the small GTPase Rac in HeLa cells.
Thus, the interaction with 14-3-3 appears to be dispensable to Par3
localization. Consistent with this, the Par3alpha-14-3-3 interaction does not
inhibit the Par3alpha-aPKC association required for the Par3alpha
localization, although the aPKC-binding site lies close to the
Ser-814-containing, 14-3-3-interacting region.",
mesh {
{
term "14-3-3 Proteins",
qual {
{
mp TRUE,
subh "metabolism"
}
}
},
{
term "Alanine",
qual {
{
subh "chemistry"
}
}
},
{
term "Alkaline Phosphatase",
qual {
{
subh "metabolism"
}
}
},
{
term "Amino Acid Sequence"
},
{
term "Animals"
},
{
term "Binding Sites"
},
{
term "Body Patterning"
},
{
term "COS Cells"
},
{
term "Carrier Proteins"
},
{
term "Cattle"
},
{
term "Cell Line"
},
{
term "Cell Lineage"
},
{
term "DNA, Complementary",
qual {
{
subh "metabolism"
}
}
},
{
term "Dogs"
},
{
term "Epithelial Cells",
qual {
{
subh "cytology"
}
}
},
{
term "Gene Library"
},
{
term "HeLa Cells"
},
{
term "Humans"
},
{
term "Immunoprecipitation"
},
{
term "Intestines",
qual {
{
subh "enzymology"
}
}
},
{
term "Membrane Proteins",
qual {
{
mp TRUE,
subh "chemistry"
}
}
},
{
term "Models, Genetic"
},
{
term "Molecular Sequence Data"
},
{
term "Mutation"
},
{
term "Phosphorylation"
},
{
term "Plasmids",
qual {
{
subh "metabolism"
}
}
},
{
term "Protein Binding"
},
{
term "Protein Structure, Tertiary"
},
{
term "Receptors, Thrombin",
qual {
{
subh "chemistry"
}
}
},
{
term "Sequence Homology, Amino Acid"
},
{
term "Serine",
qual {
{
subh "chemistry"
}
}
},
{
term "Two-Hybrid System Techniques"
}
},
substance {
{
type nameonly,
name "14-3-3 Proteins"
},
{
type nameonly,
name "Carrier Proteins"
},
{
type nameonly,
name "DNA, Complementary"
},
{
type nameonly,
name "Membrane Proteins"
},
{
type nameonly,
name "PARD3B protein, human"
},
{
type nameonly,
name "Receptors, Thrombin"
},
{
type nameonly,
name "protease-activated receptor 3"
},
{
type cas,
cit "56-41-7",
name "Alanine"
},
{
type cas,
cit "56-45-1",
name "Serine"
},
{
type ec,
cit "3.1.3.1",
name "Alkaline Phosphatase"
}
},
pmid 15721295,
pub-type {
"Journal Article",
"Research Support, Non-U.S. Gov't"
},
status medline
}
}
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