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PMID: 15081522
It (NF-KappaB) is retained in the
cytosol in a negative conformation by the inhibitory protein,
IKappaB.
PMID: 15081522
Activation of cells by appropriate stimuli activates an
upstream kinase complex comprising IKK- (IKappaB kinases-)
1 and 2 in complex with a scaffold protein IKK-gamma.
PMID: 15081522
Activation of cells by appropriate stimuli activates an
upstream kinase complex comprising IKK- (IKappaB kinases-)
1 and 2 in complex with a scaffold protein IKK-gamma.
indirect
PMID:15081522
This
results in phosphorylation of IKappaB on serines 32 and 36,
which targets it for ubiquitination and subsequent degradation.
PMID:15081522
This
results in phosphorylation of IKappaB on serines 32 and 36,
which targets it for ubiquitination and subsequent degradation.
PMID:15081522
This
results in phosphorylation of IKappaB on serines 32 and 36,
which targets it for ubiquitination and subsequent degradation.
PMID: 15081522
The NFKappaB subunits are thus released and translocate
into the nucleus where they bind their target promoters and
initiate gene transcription
PMID: 15081522
The discovery that TLR4 was the
long sought after signalling component of the lipopolysaccharide
(LPS) receptor complex (composed of CD14 and
MD2 on myeloid cells) has resulted in intense research into
how signalling pathways are regulated downstream of TLR4
PMID: 15081522
The discovery that TLR4 was the
long sought after signalling component of the lipopolysaccharide
(LPS) receptor complex (composed of CD14 and
MD2 on myeloid cells) has resulted in intense research into
how signalling pathways are regulated downstream of TLR4
PMID:15081522
The PH domain of Btk binds selectively to
the phosphatidylinositol 3-kinase (PI3K) product PIP3, any
increase in which therefore promotes membrane recruitment
of Btk.
PMID: 15081522
Importantly,
membrane targeting of Btk is the first step and a prerequisite
for its activation.
PMID:15081522
The PH domain of Btk binds selectively to
the phosphatidylinositol 3-kinase (PI3K) product PIP3, any
increase in which therefore promotes membrane recruitment
of Btk.
PMID: 15081522
With respect
to TLR4 signalling, PI3K has been shown to interact with the adaptor protein MyD88
PMID: 15081522
Specifically, MyD88 has been
shown to become tyrosine phosphorylated after LPS stimulation,
which stimulates an interaction between the newly
phosphorlyated tyrosine on MyD88 and the SH2 domain of
p85 PI3K and MyD88.
PMID:15081522
An additional
means of membrane targeting appears to be mediated
by direct interaction between the PH domain of Btk
and the G-protein beta-gamma subunits and F-actin, suggesting multiple
potential mechanisms for regulating Btk localisation
and juxtaposition with activating kinases.
PMID:15081522
An additional
means of membrane targeting appears to be mediated
by direct interaction between the PH domain of Btk
and the G-protein beta-gamma subunits and F-actin, suggesting multiple
potential mechanisms for regulating Btk localisation
and juxtaposition with activating kinases.
PMID:15081522
An additional
means of membrane targeting appears to be mediated
by direct interaction between the PH domain of Btk
and the G-protein beta-gamma subunits and F-actin, suggesting multiple
potential mechanisms for regulating Btk localisation
and juxtaposition with activating kinases.
PMID:15081522
An additional
means of membrane targeting appears to be mediated
by direct interaction between the PH domain of Btk
and the G-protein beta-gamma subunits and F-actin, suggesting multiple
potential mechanisms for regulating Btk localisation
and juxtaposition with activating kinases.
indirect
PMID: 15081522
PI3K is activated
by multiple TLR members, most notably TLR2, TLR4 and
TLR9, resulting in increased PIP3 production.
indirect
PMID: 15081522
PI3K is activated
by multiple TLR members, most notably TLR2, TLR4 and
TLR9, resulting in increased PIP3 production.
PMID: 15081522
Immunoprecipitation
experiments in the human pro-monocytic cell line,
THP-1, revealed that Btk interacted with MyD88, Mal and
IRAK-1, key proximal effectors involved in TLR4 signalling
PMID: 15081522
Immunoprecipitation
experiments in the human pro-monocytic cell line,
THP-1, revealed that Btk interacted with MyD88, Mal and
IRAK-1, key proximal effectors involved in TLR4 signalling
PMID: 15081522
Of
the 10 human TLR members, ligands for all but TLR10
have been described, with TLR2 recognising peptidoglycan,
TLR3 recognising double stranded viral RNA and TLR9
recognising bacterial hypomethylated DNA motifs, for example
PMID: 15081522
Of
the 10 human TLR members, ligands for all but TLR10
have been described, with TLR2 recognising peptidoglycan,
TLR3 recognising double stranded viral RNA and TLR9
recognising bacterial hypomethylated DNA motifs, for example
PMID: 15081522
Of
the 10 human TLR members, ligands for all but TLR10
have been described, with TLR2 recognising peptidoglycan,
TLR3 recognising double stranded viral RNA and TLR9
recognising bacterial hypomethylated DNA motifs, for example
PMID: 15081522,12471095,12539043
The third adapter identified, Trif
(also known as TICAM-1), interacts with TLR3 and mediates
TLR3-dependent induction of IFN-beta via NFKappaB
and IRF-3 activation
indirect
PMID: 15081522,12471095,12539043
The third adapter identified, Trif
(also known as TICAM-1), interacts with TLR3 and mediates
TLR3-dependent induction of IFN-beta via NFKappaB
and IRF-3 activation
indirect
PMID: 15081522,12471095,12539043
The third adapter identified, Trif
(also known as TICAM-1), interacts with TLR3 and mediates
TLR3-dependent induction of IFN-beta via NFKappaB
and IRF-3 activation
PMID: 15081522,12471095,12539043
The third adapter identified, Trif
(also known as TICAM-1), interacts with TLR3 and mediates
TLR3-dependent induction of IFN-beta via NFKappaB
and IRF-3 activation
indirect
PMID: 15081522,12471095,12539043
The third adapter identified, Trif
(also known as TICAM-1), interacts with TLR3 and mediates
TLR3-dependent induction of IFN-beta via NFKappaB
and IRF-3 activation
PMID: 15081522,14517278
Meanwhile,
a fourth adapter has recently been characterised,
TRAM (TRIF-related adaptor molecule), which, unlike any of the other adaptors, is specific for TLR4 signalling and
regulates the MyD88-independent pathway to NFKappaB and
IRF-3 activation
PMID:15081522,14556004
It also regulates late NFKappaB activation
in response to TLR4
PMID:15081522
Trif is also involved in the
MyD88-independent pathway activated by TLR4
indirect
PMID: 15081522,14517278
Meanwhile,
a fourth adapter has recently been characterised,
TRAM (TRIF-related adaptor molecule), which, unlike any of the other adaptors, is specific for TLR4 signalling and
regulates the MyD88-independent pathway to NFKappaB and
IRF-3 activation
indirect
PMID: 15081522,14517278
Meanwhile,
a fourth adapter has recently been characterised,
TRAM (TRIF-related adaptor molecule), which, unlike any of the other adaptors, is specific for TLR4 signalling and
regulates the MyD88-independent pathway to NFKappaB and
IRF-3 activation
PMID:15081522,14556004
It also regulates late NFKappaB activation
in response to TLR4
PMID: 15081522
NFkappaB is a key pro-inflammatory transcription factor activated
in response to many stimuli, perhaps the most studied
of which include LPS, IL-1 and TNFalpha
indirect
PMID: 15081522,7515809
Later work showed that Src kinases were
activated by LPS (specifically Hck and Lyn) and preceded
LPS-induced TNFalpha production in monocytes
indirect
indirect
indirect
PMID: 15081522,7515809
Later work showed that Src kinases were
activated by LPS (specifically Hck and Lyn) and preceded
LPS-induced TNFalpha production in monocytes
PMID:15081522,10565609
Other
reports directly implicated Src kinases in LPS signalling to
TNFalpha and iNOS (inducible-nitric oxide synthase) induction
with the use of the Src-selective inhibitor, PP1, in murine
macrophages
indirect
indirect
PMID:15081522,10565609
Other
reports directly implicated Src kinases in LPS signalling to
TNFalpha and iNOS (inducible-nitric oxide synthase) induction
with the use of the Src-selective inhibitor, PP1, in murine
macrophages
indirect
indirect
indirect
PMID:15081522,8258685
This was followed closely by reports showing that
PTKs were required for the induction of pro-inflammatory
cytokines (IL-1beta, IL-6 and TNFalpha) in response to LPS in
murine macrophages
indirect
indirect
indirect
PMID:15081522,8258685
This was followed closely by reports showing that
PTKs were required for the induction of pro-inflammatory
cytokines (IL-1beta, IL-6 and TNFalpha) in response to LPS in
murine macrophages
indirect
indirect
indirect
PMID:15081522,8258685
This was followed closely by reports showing that
PTKs were required for the induction of pro-inflammatory
cytokines (IL-1beta, IL-6 and TNFalpha) in response to LPS in
murine macrophages
PMID: 15081522
One of the key consequences of BCR stimulation
is activation of the transcription factor NFKappaB and consequent
induction of genes regulating cell survival and proliferation
PMID: 15081522
NFkappaB is a key pro-inflammatory transcription factor activated
in response to many stimuli, perhaps the most studied
of which include LPS, IL-1 and TNFalpha
PMID: 15081522
NFkappaB is a key pro-inflammatory transcription factor activated
in response to many stimuli, perhaps the most studied
of which include LPS, IL-1 and TNFalpha
PMID: 15081522
NFkappaB is a key pro-inflammatory transcription factor activated
in response to many stimuli, perhaps the most studied
of which include LPS, IL-1 and TNFalpha
indirect
PMID: 15081522
NFkappaB is a key pro-inflammatory transcription factor activated
in response to many stimuli, perhaps the most studied
of which include LPS, IL-1 and TNFalpha
PMID: 15081522
Immunoprecipitation
experiments in the human pro-monocytic cell line,
THP-1, revealed that Btk interacted with MyD88, Mal and
IRAK-1, key proximal effectors involved in TLR4 signalling
PMID: 15081522
Immunoprecipitation
experiments in the human pro-monocytic cell line,
THP-1, revealed that Btk interacted with MyD88, Mal and
IRAK-1, key proximal effectors involved in TLR4 signalling
indirect
PMID: 15081522,9188445
Src
kinases such as Lyn are responsible for transphosphorylation
of Btk
PMID: 15081522
This transphosphorylation event results in
the autophosphorylation of tyrosine 223 in the SH3 domain
of Btk, and subsequent activation of downstream signalling
pathways.
indirect
PMID: 15081522
However, other tyrosine kinases
are activated following TLR4 ligation—these include the
proto-oncogene Vav and kinases associated with focal adhesions
such as paxillin and focal adhesion kinase
indirect
PMID: 15081522
However, other tyrosine kinases
are activated following TLR4 ligation—these include the
proto-oncogene Vav and kinases associated with focal adhesions
such as paxillin and focal adhesion kinase
indirect
PMID: 15081522
However, other tyrosine kinases
are activated following TLR4 ligation—these include the
proto-oncogene Vav and kinases associated with focal adhesions
such as paxillin and focal adhesion kinase
PMID: 15081522,9763609
Following
BCR-induced activation of Btk, PLCgamma becomes phosphorylated
with subsequent production of IP3, mobilisation of
intracellular Ca2+ stores and activation of PKC via diacylglycerol
(DAG).
PMID:15081522
A number
of proteins have been identified that bind Btk and negatively
regulate its function. These include the recently identified
IBtk (inhibitor of Btk), a 26 kDa protein identified in
a yeast-two-hybrid screen using Btk as a bait.
PMID:15081522
Another
negative regulator of Btk activity is the protein Sab, which
binds the SH3 domain of Btk (constitutively) and directly inhibits
kinase activity.
PMID: 15081522,7629518
The SH3 domain of Btk has also been
shown to interact with c-Cbl, a multi-domain-containing
protein.
c-Cbl may also function to negatively regulate Btk activity
in cells
indirect
PMID: 15081522,9763609
Following
BCR-induced activation of Btk, PLCgamma becomes phosphorylated
with subsequent production of IP3, mobilisation of
intracellular Ca2+ stores and activation of PKC via diacylglycerol
(DAG).
indirect
PMID: 15081522,9763609
Following
BCR-induced activation of Btk, PLCgamma becomes phosphorylated
with subsequent production of IP3, mobilisation of
intracellular Ca2+ stores and activation of PKC via diacylglycerol
(DAG).
indirect
PMID: 15081522,9763609
Following
BCR-induced activation of Btk, PLCgamma becomes phosphorylated
with subsequent production of IP3, mobilisation of
intracellular Ca2+ stores and activation of PKC via diacylglycerol
(DAG).
PMID: 15081522,9763609
Following
BCR-induced activation of Btk, PLCgamma becomes phosphorylated
with subsequent production of IP3, mobilisation of
intracellular Ca2+ stores and activation of PKC via diacylglycerol
(DAG).
indirect
PMID: 15081522
Btk deficient cells also show defects in
JNK and p38 MAPK activation, indicating a role for Btk
upstream on the pathways regulating their activation
indirect
PMID: 15081522
Btk deficient cells also show defects in
JNK and p38 MAPK activation, indicating a role for Btk
upstream on the pathways regulating their activation
indirect
PMID:15081522
These and other pathways activated
by Btk lead to the activation of transcription factors,
principally NFKappaB, and AP-1, which are responsible for mediating
the induction of genes required for B cell survival and
proliferation.
indirect
PMID:15081522
These and other pathways activated
by Btk lead to the activation of transcription factors,
principally NFKappaB, and AP-1, which are responsible for mediating
the induction of genes required for B cell survival and
proliferation.
PMID:15081522
Using its SH2 domain Btk binds the adaptor protein
BLNK/SLP-65 (in B cells), which serves as a scaffold for
binding PLC-gamma, Vav and Grb-2, each of which is responsible
for activating individual downstream pathways
PMID:15081522
Using its SH2 domain Btk binds the adaptor protein
BLNK/SLP-65 (in B cells), which serves as a scaffold for
binding PLC-gamma, Vav and Grb-2, each of which is responsible
for activating individual downstream pathways
PMID:15081522
Using its SH2 domain Btk binds the adaptor protein
BLNK/SLP-65 (in B cells), which serves as a scaffold for
binding PLC-gamma, Vav and Grb-2, each of which is responsible
for activating individual downstream pathways
PMID:15081522,9012831,10373551,11120822
A more direct involvement in transcriptional
regulation has been suggested from the observation that Btk
can interact with the transcription factors BAP135/TFII-I
and Bright, and regulate their activation
PMID:15081522
Btk is also
activated by receptors other than TLR4 and the BCR, including
the receptors for IL-3, IL-5 and IL-6, G protein coupled
receptors (GPCR) and FcepsilonRI receptors on mast cells
PMID: 15081522
However, given the ability
of Btk to associate with TLR4 and key proximal signalling
components of the receptor complex it is possible that these
interactions promote membrane localisation and Btk activation.
PMID:15081522
Btk is also
activated by receptors other than TLR4 and the BCR, including
the receptors for IL-3, IL-5 and IL-6, G protein coupled
receptors (GPCR) and FcepsilonRI receptors on mast cells
indirect
PMID:15081522
Btk is also
activated by receptors other than TLR4 and the BCR, including
the receptors for IL-3, IL-5 and IL-6, G protein coupled
receptors (GPCR) and FcepsilonRI receptors on mast cells
indirect
PMID:15081522
Btk is also
activated by receptors other than TLR4 and the BCR, including
the receptors for IL-3, IL-5 and IL-6, G protein coupled
receptors (GPCR) and FcepsilonRI receptors on mast cells
PMID:15081522
Btk is also
activated by receptors other than TLR4 and the BCR, including
the receptors for IL-3, IL-5 and IL-6, G protein coupled
receptors (GPCR) and FcepsilonRI receptors on mast cells
PMID:15081522
Btk is also
activated by receptors other than TLR4 and the BCR, including
the receptors for IL-3, IL-5 and IL-6, G protein coupled
receptors (GPCR) and FcepsilonRI receptors on mast cells
indirect
PMID:15081522
Btk is also
activated by receptors other than TLR4 and the BCR, including
the receptors for IL-3, IL-5 and IL-6, G protein coupled
receptors (GPCR) and FcepsilonRI receptors on mast cells
PMID:15081522
Btk is also
activated by receptors other than TLR4 and the BCR, including
the receptors for IL-3, IL-5 and IL-6, G protein coupled
receptors (GPCR) and FcepsilonRI receptors on mast cells
indirect
PMID:15081522
Btk is also
activated by receptors other than TLR4 and the BCR, including
the receptors for IL-3, IL-5 and IL-6, G protein coupled
receptors (GPCR) and FcepsilonRI receptors on mast cells
PMID:15081522
A number
of proteins have been identified that bind Btk and negatively
regulate its function. These include the recently identified
IBtk (inhibitor of Btk), a 26 kDa protein identified in
a yeast-two-hybrid screen using Btk as a bait.
PMID:15081522
Another
negative regulator of Btk activity is the protein Sab, which
binds the SH3 domain of Btk (constitutively) and directly inhibits
kinase activity.
PMID: 15081522,7629518
The SH3 domain of Btk has also been
shown to interact with c-Cbl, a multi-domain-containing
protein.
c-Cbl may also function to negatively regulate Btk activity
in cells
PMID:15081522,9012831,10373551,11120822
A more direct involvement in transcriptional
regulation has been suggested from the observation that Btk
can interact with the transcription factors BAP135/TFII-I
and Bright, and regulate their activation
indirect
PMID:15081522,10811867
BCR stimulation
also failed to activate IKappaB kinase (IKK) in these
cells, suggesting that Btk is required for activation of IKK
downstream of the BCR
indirect
PMID: 15081522
PI3K is activated
by multiple TLR members, most notably TLR2, TLR4 and
TLR9, resulting in increased PIP3 production.
indirect
PMID: 15081522
PI3K is activated
by multiple TLR members, most notably TLR2, TLR4 and
TLR9, resulting in increased PIP3 production.
PMID: 15081522
Further analysis
revealed that Btk interacted with the TIR domain of TLR4,
the receptor for Gram negative LPS.
PMID:15081522,12724322
In confirmation of a putative role for Btk downstream of
TLRs, we have identified the TIR domain of TLR8 as a Btk
interactor in a yeast-two-hybrid screen
indirect
PMID: 15081522
Specifically, MyD88 has been
shown to become tyrosine phosphorylated after LPS stimulation,
which stimulates an interaction between the newly
phosphorlyated tyrosine on MyD88 and the SH2 domain of
p85 PI3K and MyD88.
PMID: 15081522
Using its SH2 domain Btk binds the adaptor protein
BLNK/SLP-65 (in B cells), which serves as a scaffold for
binding PLC-gamma, Vav and Grb-2, each of which is responsible
for activating individual downstream pathways.
PMID: 15081522
Using its SH2 domain Btk binds the adaptor protein
BLNK/SLP-65 (in B cells), which serves as a scaffold for
binding PLC-gamma, Vav and Grb-2, each of which is responsible
for activating individual downstream pathways.