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Phosphorylation of a heme-regulated eukaryotic initiation factor 2α kinase enhances the interaction with heat-shock protein 90 and substantially upregulates kinase activity.
[erythropoietic protoporphyria]
Heme-regulated
eukaryotic
initiation
factor
2
α
kinase
(
HRI
)
functions
under
conditions
of
heme
shortage
caused
by
blood
diseases
such
as
erythropoietic
protoporphyria
and
β-thalassemia
,
and
retains
the
heme
:
globin
ratio
at
1
:
1
by
sensing
the
heme
concentration
in
reticulocytes
.
This
HRI
function
is
regulated
by
various
factors
including
autophosphorylation
and
protein-protein
interactions
.
A
heat-shock
protein
controls
HRI
function
,
however
,
the
molecular
mechanism
of
catalytic
regulation
of
HRI
by
the
heat-shock
protein
is
unclear
.
In
the
present
study
,
we
examined
the
interactions
of
HRI
with
a
heat-shock
protein
,
Hsp
90
,
under
various
conditions
,
using
a
pull-down
assay
and
measuring
catalytic
activity
.
It
was
found
that
[
1
]
an
interaction
between
Hsp
90
and
phosphorylated
HRI
was
evident
,
whereas
no
interaction
was
observed
between
Hsp
90
and
HRI
dephosphorylated
by
treatment
with
λ
protein
phosphatase
;
[
2
]
Hsp
90
enhanced
the
kinase
activity
of
phosphorylated
HRI
but
not
dephosphorylated
HRI
,
but
this
enhancement
was
not
observed
in
the
presence
of
heme
;
and
,
[
3
]
autophosphorylation
of
HRI
was
not
influenced
by
Hsp
90
.
Therefore
,
we
propose
that
autophosphorylation
of
HRI
is
critical
for
catalytic
regulation
by
Hsp
90
under
heme-shortage
conditions
.
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Diseases presenting
"β-thalassemia"
symptom
erythropoietic protoporphyria
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