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PMID: 11073096,10427991,9704038
Cells are responsive to bacterial components, leukotrienes, complement factors, and chemokines, an ever-expanding family of attractants controlling leukocyte migration. All these attractants in both neutrophils and monocytes/macrophages interact with specific serpentine (heptahelical) receptors [13 ], embedded in the plasma membrane, that transduce ligand-induced signals by coupling to heterotrimeric G proteins
PMID: 11073096,10427991,9704038
Cells are responsive to bacterial components, leukotrienes, complement factors, and chemokines, an ever-expanding family of attractants controlling leukocyte migration. All these attractants in both neutrophils and monocytes/macrophages interact with specific serpentine (heptahelical) receptors [13 ], embedded in the plasma membrane, that transduce ligand-induced signals by coupling to heterotrimeric G proteins
PMID: 11073096,10427991,9704038
Cells are responsive to bacterial components, leukotrienes, complement factors, and chemokines, an ever-expanding family of attractants controlling leukocyte migration. All these attractants in both neutrophils and monocytes/macrophages interact with specific serpentine (heptahelical) receptors [13 ], embedded in the plasma membrane, that transduce ligand-induced signals by coupling to heterotrimeric G proteins
PMID: 11073096
In the GDP-bound form, the {alpha} subunit interacts with the ß and {gamma} subunits to form an inactive heterotrimer that binds to the serpentine receptor
PMID: 11073096,10427991,9704038
Cells are responsive to bacterial components, leukotrienes, complement factors, and chemokines, an ever-expanding family of attractants controlling leukocyte migration. All these attractants in both neutrophils and monocytes/macrophages interact with specific serpentine (heptahelical) receptors [13 ], embedded in the plasma membrane, that transduce ligand-induced signals by coupling to heterotrimeric G proteins
PMID: 11073096
Heterotrimeric G-proteins are made up of an {alpha}, beta, and {gamma} subunit, with the {alpha} subunit being the GDP/GTP binding module.
PMID: 11073096
In the GDP-bound form, the {alpha} subunit interacts with the beta and {gamma} subunits to form an inactive heterotrimer that binds to the serpentine receptor
PMID: 11073096
Ligand (chemokine) binding to the receptor induces a conformational change that results in exchange of GDP for GTP on the {alpha} subunit, inducing its dissociation from both the receptor and the Gbeta{gamma} subunit.
PMID: 11073096
Ligand (chemokine) binding to the receptor induces a conformational change that results in exchange of GDP for GTP on the {alpha} subunit, inducing its dissociation from both the receptor and the Gbeta{gamma} subunit.
PMID: 11073096
Ligand (chemokine) binding to the receptor induces a conformational change that results in exchange of GDP for GTP on the {alpha} subunit, inducing its dissociation from both the receptor and the Gbeta{gamma} subunit.
PMID: 11073096
Ligand (chemokine) binding to the receptor induces a conformational change that results in exchange of GDP for GTP on the {alpha} subunit, inducing its dissociation from both the receptor and the Gbeta{gamma} subunit.
PMID: 11073096
Ligand (chemokine) binding to the receptor induces a conformational change that results in exchange of GDP for GTP on the {alpha} subunit, inducing its dissociation from both the receptor and the Gbeta{gamma} subunit.
PMID: 11073096
Ligand (chemokine) binding to the receptor induces a conformational change that results in exchange of GDP for GTP on the {alpha} subunit, inducing its dissociation from both the receptor and the Gbeta{gamma} subunit.
PMID: 11073096
Ligand (chemokine) binding to the receptor induces a conformational change that results in exchange of GDP for GTP on the {alpha} subunit, inducing its dissociation from both the receptor and the Gbeta{gamma} subunit.
PMID: 11073096
Ligand (chemokine) binding to the receptor induces a conformational change that results in exchange of GDP for GTP on the {alpha} subunit, inducing its dissociation from both the receptor and the Gbeta{gamma} subunit.
PMID: 11073096
The G protein complex dissociates into {alpha} and ß{gamma} subunits, which in turn bind and activate target enzymes such as phospholipase C, phosphoinositide 3-kinase (PI 3-kinase), or adenyl cyclase.
PMID: 11073096
The G protein complex dissociates into {alpha} and ß{gamma} subunits, which in turn bind and activate target enzymes such as phospholipase C, phosphoinositide 3-kinase (PI 3-kinase), or adenyl cyclase.
PMID: 11073096
The G protein complex dissociates into {alpha} and ß{gamma} subunits, which in turn bind and activate target enzymes such as phospholipase C, phosphoinositide 3-kinase (PI 3-kinase), or adenyl cyclase.
PMID: 11073096
The G protein complex dissociates into {alpha} and ß{gamma} subunits, which in turn bind and activate target enzymes such as phospholipase C, phosphoinositide 3-kinase (PI 3-kinase), or adenyl cyclase.
PMID: 11073096
The G protein complex dissociates into {alpha} and ß{gamma} subunits, which in turn bind and activate target enzymes such as phospholipase C, phosphoinositide 3-kinase (PI 3-kinase), or adenyl cyclase.
PMID: 11073096
The G protein complex dissociates into {alpha} and ß{gamma} subunits, which in turn bind and activate target enzymes such as phospholipase C, phosphoinositide 3-kinase (PI 3-kinase), or adenyl cyclase.
PMID:11073096,10579926
At least four Class I PI 3-kinase isoforms exist in mammalian cells, but only one form, a single Class IB variant containing the p110{gamma} catalytic subunit complexed with a 101-kDa regulatory protein, is thought to interact with G-proteins in leukocytes.
PMID:11073096
he free G{alpha} and Gß{gamma} subunits then interact with and modulate the activity of target proteins such as the Class 1B p101/p110{gamma} PI 3-kinase.
indirect
PMID: 11073096
Whatever the case, all appear to converge on a common pathway where the outcome will lead to the phosphorylation of phosphatidylinositol-4,5-bisphosphate (PIP2) by activated PI 3-kinase. As a result, phosphatidylinositol-3,4,5-triphosphate (PIP3) is generated
indirect
PMID: 11073096
Whatever the case, all appear to converge on a common pathway where the outcome will lead to the phosphorylation of phosphatidylinositol-4,5-bisphosphate (PIP2) by activated PI 3-kinase. As a result, phosphatidylinositol-3,4,5-triphosphate (PIP3) is generated
PMID: 11073096
Homodimers of cytokine (such as CSF-1) induce a rapid sequence of changes.
PMID: 11073096
Ligand-induced covalent dimerization of receptor leads to autophosphorylation at a number of tyrosine residues on the cytoplasmic tail, which initiates signaling events that precede the rapid internalization and subsequent degradation of receptor-ligand complexes
PMID: 11073096
Ligand-induced covalent dimerization of receptor leads to autophosphorylation at a number of tyrosine residues on the cytoplasmic tail, which initiates signaling events that precede the rapid internalization and subsequent degradation of receptor-ligand complexes
PMID: 11073096
Ligand-induced covalent dimerization of receptor leads to autophosphorylation at a number of tyrosine residues on the cytoplasmic tail, which initiates signaling events that precede the rapid internalization and subsequent degradation of receptor-ligand complexes
PMID: 11073096,8947469
Unlike serpentine receptors, receptor tyrosine kinases such as CSF-1R directly interact with a host of substrates after autophosphorylation induced by ligand binding, although in CSF-1-treated mouse macrophages, PI 3-kinase is the major protein associated with the activated receptor
PMID: 11073096
The p110 subunits in these PI 3-kinases exist in complex with a p85 protein that has two Src-homology-2 (SH2) domains
PMID: 11073096,10754559
The latter bind to phosphorylated tyrosine residues found on activated CSF-1R, thus allowing translocation to the plasma membrane where their lipid (such as PIP2) and other substrates are found
PMID: 11073096
As was described for serpentine receptors, the net result of PI 3-kinase activation through receptor tyrosine kinases is the generation of PIP3
PMID: 11073096
Once again, recruitment to the plasma membrane of any of the p110 catalytic subunits results in the generation of PIP3
PMID: 11073096,7737969
It was shown earlier that CSF-1R induces direct interaction of PI 3-kinase (via its p85 subunit) with the SH2/SH3 adaptor protein Grb2
indirect
PMID: 11073096,1643657
The most frequently used tool for studying Rho function is C3 transferase, an exoenzyme from Clostridium botulinum, which ADP-ribosylates and inactivates Rho
PMID: 11073096,1643657
The most frequently used tool for studying Rho function is C3 transferase, an exoenzyme from Clostridium botulinum, which ADP-ribosylates and inactivates Rho
PMID: 11073096,8990121
In the case of Vav, a GEF expressed only in hematopoietic cells, there is good evidence for this hypothesis because Vav is activated by tyrosine phosphorylation in response to extracellular signals, and binding of PIP3 enhances this phosphorylation
PMID: 11073096,9268346
PIP3 binds to the PH domain of at least three GEFs, Tiam1, Sos, and the leukocyte-specific Vav
indirect
indirect
PMID: 11073096,8990121
In the case of Vav, a GEF expressed only in hematopoietic cells, there is good evidence for this hypothesis because Vav is activated by tyrosine phosphorylation in response to extracellular signals, and binding of PIP3 enhances this phosphorylation
PMID:11073096,7888179,10081066
Finally, Rho, Rac, and Cdc42 have all been shown to complex with proteins known as GDIs (guanine nucleotide dissociation inhibitors), which prevent their interaction with other regulatory proteins and keep them sequestered in the cytoplasm
PMID: 11073096,9490022
Of the three mammalian GDIs specific for the Rho family, only RhoGDI has a high affinity for RhoA, Rac1, and Cdc42
PMID: 11073096,8858161
In addition to keeping Rho family proteins in an inactive complex in the cytoplasm, RhoGDI interacts with ERM (ezrin/radixin/moesin) proteins, which in turn interact with transmembrane proteins such as CD44 and ICAM-1, and also with actin
PMID: 11073096,8858161
In addition to keeping Rho family proteins in an inactive complex in the cytoplasm, RhoGDI interacts with ERM (ezrin/radixin/moesin) proteins, which in turn interact with transmembrane proteins such as CD44 and ICAM-1, and also with actin
PMID: 11073096,8858161
In addition to keeping Rho family proteins in an inactive complex in the cytoplasm, RhoGDI interacts with ERM (ezrin/radixin/moesin) proteins, which in turn interact with transmembrane proteins such as CD44 and ICAM-1, and also with actin
PMID: 11073096,8858161
In addition to keeping Rho family proteins in an inactive complex in the cytoplasm, RhoGDI interacts with ERM (ezrin/radixin/moesin) proteins, which in turn interact with transmembrane proteins such as CD44 and ICAM-1, and also with actin
PMID: 11073096,9681826
ERM proteins can also bind to the Rho GEF, Dbl, suggesting that they may coordinate the release of Rho proteins from GDIs and enhance exchange of GDP for GTP
PMID: 11073096,9681826
ERM proteins can also bind to the Rho GEF, Dbl, suggesting that they may coordinate the release of Rho proteins from GDIs and enhance exchange of GDP for GTP
indirect
PMID: 11073096,9099945
Rac is activated by a wide variety of tyrosine kinase receptors including the CSF-1R and serpentine receptors .
PMID: 11073096,9268346
PIP3 binds to the PH domain of at least three GEFs, Tiam1, Sos, and the leukocyte-specific Vav
PMID: 11073096,9268346
PIP3 binds to the PH domain of at least three GEFs, Tiam1, Sos, and the leukocyte-specific Vav
PMID: 11073096,8810279
It should not be forgotten that many other possibilities exist. It has been shown that N-formyl-methionyl-leucyl-phenylalanine (fMLP) receptor stimulation will also cause activation of the src-related kinase, Lyn, directly indicating the involvement of tyrosine kinase activity leading to Rac and Cdc42 activation through serpentine receptor activation.
indirect
PMID: 11073096,8810279
It should not be forgotten that many other possibilities exist. It has been shown that N-formyl-methionyl-leucyl-phenylalanine (fMLP) receptor stimulation will also cause activation of the src-related kinase, Lyn, directly indicating the involvement of tyrosine kinase activity leading to Rac and Cdc42 activation through serpentine receptor activation.
PMID: 11073096,8756646
For example, IQGAP1, which is abundant in lamellipodia, binds to actin filaments and also to Rac and Cdc42
PMID: 11073096,8756646
For example, IQGAP1, which is abundant in lamellipodia, binds to actin filaments and also to Rac and Cdc42
PMID: 11073096,9210375
A Cdc42-interacting protein, CIP4, shows sequence homology to a small region of ERM proteins and may act as a transducer to the actin cytoskeleton
indirect
PMID: 11073096,10081063,9037011
In addition, Rho-kinase/ROK can induce the phosphorylation of myosin II light chain kinase, whereas the Rac/Cdc42-specific PAK family of kinases can phosphorylate myosin I heavy chain, although it is debatable whether this occurs in mammalian cells
indirect
PMID: 11073096,10081063,9037011
In addition, Rho-kinase/ROK can induce the phosphorylation of myosin II light chain kinase, whereas the Rac/Cdc42-specific PAK family of kinases can phosphorylate myosin I heavy chain, although it is debatable whether this occurs in mammalian cells
PMID: 11073096,9214622
Finally, the Rho target p140mDia can bind to profilin, an actin-binding protein with the potential to enhance actin polymerization at the leading edge of migrating cells.
indirect
PMID: 11073096,8805223,8643625,8625410
Three groups have demonstrated that WASP interacts directly with Cdc42 in a GTP-dependent manner
PMID: 11073096,9822597
Just carboxy-terminal to the EVH1 domain of WASP is the CRIB motif, which confers interaction with Cdc42, and more centrally there are proline-rich sequences that can interact with SH3-containing proteins such as the adaptor proteins Nck and Grb2, protein tyrosine kinases of the c-Src family such as Fyn, and the actin-binding protein profilin
PMID: 11073096,9822597
Just carboxy-terminal to the EVH1 domain of WASP is the CRIB motif, which confers interaction with Cdc42, and more centrally there are proline-rich sequences that can interact with SH3-containing proteins such as the adaptor proteins Nck and Grb2, protein tyrosine kinases of the c-Src family such as Fyn, and the actin-binding protein profilin
PMID: 11073096,9822597
Just carboxy-terminal to the EVH1 domain of WASP is the CRIB motif, which confers interaction with Cdc42, and more centrally there are proline-rich sequences that can interact with SH3-containing proteins such as the adaptor proteins Nck and Grb2, protein tyrosine kinases of the c-Src family such as Fyn, and the actin-binding protein profilin
PMID: 11073096,9822597
Just carboxy-terminal to the EVH1 domain of WASP is the CRIB motif, which confers interaction with Cdc42, and more centrally there are proline-rich sequences that can interact with SH3-containing proteins such as the adaptor proteins Nck and Grb2, protein tyrosine kinases of the c-Src family such as Fyn, and the actin-binding protein profilin
PMID: 11073096,9822597
Just carboxy-terminal to the EVH1 domain of WASP is the CRIB motif, which confers interaction with Cdc42, and more centrally there are proline-rich sequences that can interact with SH3-containing proteins such as the adaptor proteins Nck and Grb2, protein tyrosine kinases of the c-Src family such as Fyn, and the actin-binding protein profilin
PMID: 11073096,9889097
The second is the A motif, which includes a cluster of acidic residues that mediate binding to the Arp2/3 complex
indirect
PMID: 11073096,10224076
Rac is activated by a wide variety of tyrosine kinase receptors including the CSF-1R and serpentine receptors