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1
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0027397544
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Inositol triphosphate and calcium signaling
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(1993)
Nature
, vol.361
, pp. 315-325
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-
Berridge1
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3
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0028274104
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Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly
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2+ and the polyphosphoinositide lipids phosphatidylinositol (4)-phosphate and phosphatidylinositol (4,5)-bisphosphate on proteins or protein complexes that affect the state of actin assembly. Janmey attempts to integrate the data on individual proteins to suggest a possible set of coordinated reactions that could produce the assembly/disassembly of the actin network in vivo. This review should be read in conjunction with [51].
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(1994)
Annu Rev Physiol
, vol.56
, pp. 169-191
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Janmey1
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4
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0027965240
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Novel function of phosphatidylinositol 4,5-bisphosphate as a cofactor for brain membrane phospholipase D
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2 is predicted to form part of a general mechanism for membrane vesiculation and/or fusion.
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(1994)
J Biol Chem
, vol.269
, pp. 21403-21406
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Liscovitch1
Chalifa2
Pertile3
Chen4
Cantley5
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5
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0028021882
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Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
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2 is a membrane-attachment site for proteins containing PH domains.
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(1994)
Nature
, vol.371
, pp. 168-170
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Harlan1
Hajduk2
Yoon3
Fesik4
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6
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0026654469
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Regulation of inositol phospholipid-specific phospholipase C isozymes.
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(1992)
J Biol Chem
, vol.267
, pp. 12393-12396
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Rhee1
Choi2
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7
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0024403320
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Studies of inositol phospholipid-specific phospholipase C
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(1989)
Science
, vol.244
, pp. 546-550
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Rhee1
Suh2
Ryu3
Lee4
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14
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0027980089
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PH domains and phospholipases — a meaningful relationship?
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of special interest, The sequence alignments of isozymes of phospholipase C reveal the presence of a pleckstrin homology domain at the amino terminus.
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(1994)
Trends Biochem Sci
, vol.19
, pp. 54-55
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Parker1
Hemmings2
Gierschik3
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16
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0027523306
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Phosphorylation sites at the C-terminus of the platelet-derived growth factor receptor bind phospholipase Cγ1
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(1993)
Mol Biol Cell
, vol.4
, pp. 49-57
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Kashishian1
Cooper2
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21
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0028277954
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Individual epidermal growth factor receptor autophosphorylation sites do not stringently define association motifs for several SH2-containing proteins
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(1994)
J Biol Chem
, vol.269
, pp. 12320-12324
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Soler1
Beguinot2
Carpenter3
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24
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0027211693
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Phospholipase C-γ1 and phosphatidylinositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal
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(1993)
Cell
, vol.73
, pp. 321-334
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Valilus1
Kazlauskas2
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28
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0028263973
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Epidermal growth factor-induced activation and translocation of phospholipase C-γ1 to the cytoskeleton in rat hepatocytes
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of special interest, The authors report the relationship between the tyrosine phosphorylation of phospholipase C (PLC)-γ1 induced by epidermal growth factor (EGF) and its translocation from the cytosol to the Triton X-100 insoluble cytoskeletal fraction in rat hepatocytes. The translocation of PLC-γ1 is a specific effect of EGF stimulation, because a similar effect is not observed with insulin and vasopressin. Tyrosine-phosphorylated PLC-γ1 is seen only in the cytoskeletal fraction, suggesting that tyrosine phosphorylation is required for PlC-γ1 translocation to the cytoskeleton.
-
(1994)
J Biol Chem
, vol.269
, pp. 7156-7162
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-
Yang1
Rhee2
Williamson3
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29
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0027170920
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SH3 domains direct cellular localization of signaling molecules
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of special interest, This paper describes the cellular distribution of the Src homology (SH)2 and SH3 domains of phospholipase C (PLC)-γ1 and Grb2 following their microinjection into living rat embryo fibroblasts. Immunofluorescence microscopy shows that a truncated protein composed of the SH2 and SH3 domains of PLC-γ1 is localized to the actin cytoskeleton. A similar localization pattern is observed when only the SH3 domain of PLC-γ1 is microinjected. In contrast, a truncated protein composed of only the SH2 domains of PLC-γ1 exhibits diffuse cytoplasmic distribution. These results indicate that the SH3 domain is responsible for the targeting of PLC-γ1 to the actin cytoskeleton.
-
(1993)
Cell
, vol.74
, pp. 83-91
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-
Bar-Sagi1
Rotin2
Batzer3
Mandiyan4
Schlessinger5
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30
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0028279791
-
Ciliary neutrophic factor/leukemia inhibitory factor/interleukin 6/oncostatin M family of cytokines induces tyrosine phosphorylation of a common set of proteins overlapping those induced by other cytokines and growth factors
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(1994)
J Biol Chem
, vol.269
, pp. 11648-11655
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Boulton1
Stahl2
Yancopoulos3
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37
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0025724957
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q subfamily of guanine nucleotide-binding regulatory protein α subunits attenuate activation of phosphatidylinositol 4,5-bisphosphate hydrolysis by hormones
-
(1991)
J Biol Chem
, vol.266
, pp. 20519-20524
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-
Gutowski1
Smrcka2
Nowak3
Wu4
Simon5
Sternweis6
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39
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0026446880
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Activation of cytosolic phosphoinositide phospholipase C by G-protein βγ subunits
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(1992)
J Biol Chem
, vol.267
, pp. 23069-23075
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Blank1
Brattain2
Exton3
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42
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0027214868
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Regulation of purified subtypes of PLC-β by G protein α and βγ subunits
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(1993)
J Biol Chem
, vol.268
, pp. 9667-9674
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Smrcka1
Sternweis2
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44
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0028246440
-
Binding of G protein βγ-subunits to pleckstrin homology domains
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of outstanding interest, Glutathione S-transferase fusion proteins containing the pleckstrin homology (PH) domains from a variety of proteins, including β-adrenergic receptor kinase, phospholipase C-γ1, and pleckstrin, are constructed. These fusion proteins bind Gβγ to varying extents. Studies with a series of truncated PH domains indicate that the Gβγ binding domain includes only the carboxy-terminal portion of the PH domain and sequences just outside it. This paper also shows that the binding of Gβγ to Gα and the fusion proteins containing PH domains is mutually exclusive. This paper should be read together with [45], which demonstrates that the PH domain of Bruton tyrosine kinase also interacts with Gβγ and that a highly conserved tryptophan in the carboxy-terminal portion of the PH domain is critical for this interaction.
-
(1994)
J Biol Chem
, vol.269
, pp. 10217-10220
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Touhara1
Inglese2
Pitcher3
Shaw4
Lefkowitz5
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47
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0028175956
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v-src monoclonal antibody inhibits activation of phospholipase C in platelets
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(1994)
J Biol Chem
, vol.269
, pp. 9123-9127
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Dhar1
Shukla2
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48
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0027185354
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An essential role for phosphatidylinositol transfer protein in phospholipase C-mediated inositol lipid signaling
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of outstanding interest, When cytosolic components are allowed to leak out of permeabilized HL60 cells, the G protein stimulated phospholipase C (PLC) activity is greatly diminished, indicating an essential role for cytosolic component(s). One of the components is purified on the basis of its capacity to reconstitute PLC activity mediated by the non-hydrolyzable GTP analogue GTPγS and identified as the phosphatidylinositol transfer protein. On the basis of this in vitro effect of the transfer protein, the authors propose that it is involved in transporting phosphatidylinositol from intracellular compartments for conversion to phosphatidylinositol (4,5)-bisphosphate before its hydrolysis by PLC-β isozymes.
-
(1993)
Cell
, vol.74
, pp. 919-928
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Thomas1
Cunningham2
Fensome3
Ball4
Totty5
Truong6
Hsuan7
Cockcroft8
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51
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0028174102
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2-binding proteins involved in signaling by tyrosine kinase
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2 staining in these areas. In addition, the thick microfilament bundles and focal contacts disappear within 15 min of PDGF stimulation.
-
(1994)
J Biol Chem
, vol.269
, pp. 1518-1522
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Fukami1
Endo2
Imamura3
Takenawa4
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56
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0028171403
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Activation of phospholipase C-γ is necessary for stimulation of phospholipase D by platelet-derived growth factor
-
(1994)
J Biol Chem
, vol.269
, pp. 27823-27826
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Yeo1
Kazlauskas2
Exton3
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57
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0028034025
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Activation of phospholipase D induced by platelet-derived growth factor is dependent upon the level of phospholipase C-γ1
-
(1994)
J Biol Chem
, vol.269
, pp. 26843-26847
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-
Lee1
Kim2
Pai3
Ryu4
Suh5
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