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Article ; Online: Wnt signalling: the case of the 'missing' G-protein.

Malbon, Craig C

2011 Volume 433, Issue 3, Page(s) e3–5

Abstract: Wnt signalling remains a hot topic for cell signalling sleuthhounds. The trail of signalling downstream of the seven-transmembrane segment Frizzleds, which bind Wnt ligands, is replete of clues [e.g. LPR5/6 (lipoprotein receptor-related protein 5/6), G- ... ...

Abstract	Wnt signalling remains a hot topic for cell signalling sleuthhounds. The trail of signalling downstream of the seven-transmembrane segment Frizzleds, which bind Wnt ligands, is replete of clues [e.g. LPR5/6 (lipoprotein receptor-related protein 5/6), G-proteins or Dishevelled] and yet remains the 'final problem'. Although the heptahelical nature of Frizzleds places them well within a populous family of G-protein-coupled receptors, resistance to this theme has waxed and waned amid increasing demands for 'proof'. The Wnt Homepage (http://www.stanford.edu/group/nusselab/cgi-bin/wnt/) has acted as a dynamic real-time arbiter of the controversy, highlighted by the appearance and later the disappearance of the G-protein from its central diagramming and tabulations. A recent publication in this issue of the Biochemical Journal offers a solution to the 'final problem', demonstrating under native conditions that Frizzleds expressed in mammalian brain preparations act functionally to catalyse guanine-nucleotide exchange in response to stimulation with Wnt3a. Lensed from the fictional character of Sherlock Holmes, The Case of the Missing G-Protein is investigated.
MeSH term(s)	Animals ; Frizzled Receptors/physiology ; GTP-Binding Proteins/metabolism ; Guanine Nucleotides/metabolism ; Humans ; Signal Transduction ; Wnt Proteins/metabolism
Chemical Substances	Frizzled Receptors ; Guanine Nucleotides ; Wnt Proteins ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2011-02-01
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BJ20102111
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Article: A-kinase anchoring proteins: trafficking in G-protein-coupled receptors and the proteins that regulate receptor biology.

Malbon, Craig C

Current opinion in drug discovery & development

2007 Volume 10, Issue 5, Page(s) 573–579

Abstract: Scaffold proteins, such as members of the A-kinase anchoring protein (AKAP) family, constitute molecular 'tool boxes' that assist in modulating the amplitude, integration and transduction of information along signaling pathways. As AKAPs are multivalent ... ...

Abstract	Scaffold proteins, such as members of the A-kinase anchoring protein (AKAP) family, constitute molecular 'tool boxes' that assist in modulating the amplitude, integration and transduction of information along signaling pathways. As AKAPs are multivalent and often display trafficking in response to the activation of a signaling pathway, each represents a scaffold with multiple, high-value targets for new drug discovery. Recent efforts at the molecular description of a subset of AKAPs that dynamically interact with members of the superfamily of G-protein-coupled receptors and ion channels provide an ideal starting point for drug discovery and development, one that has already produced a lead-like compound. Each of the docking sites for receptors/channels, protein kinases, phosphoprotein phosphatases and adaptor molecules may prove to be a suitable candidate for molecular description and for the identification of small molecules that can interfere with and/or modulate the activity of the overall signaling pathway, providing benefits to health or in treating disease states.
MeSH term(s)	A Kinase Anchor Proteins/chemistry ; A Kinase Anchor Proteins/metabolism ; Amino Acid Sequence ; Animals ; Drug Design ; Humans ; Macromolecular Substances/chemistry ; Macromolecular Substances/metabolism ; Molecular Sequence Data ; Protein Transport ; Receptors, G-Protein-Coupled/chemistry ; Receptors, G-Protein-Coupled/metabolism ; Signal Transduction
Chemical Substances	A Kinase Anchor Proteins ; Macromolecular Substances ; Receptors, G-Protein-Coupled
Language	English
Publishing date	2007-09
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1461136-3
ISSN	2040-3437 ; 1367-6733
ISSN (online)	2040-3437
ISSN	1367-6733
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Article ; Online: Wnt3a-stimulated LRP6 phosphorylation is dependent upon arginine methylation of G3BP2.

Bikkavilli, Rama Kamesh / Malbon, Craig C

Journal of cell science

2012 Volume 125, Issue Pt 10, Page(s) 2446–2456

Abstract: Wnt signaling is initiated upon binding of Wnt proteins to Frizzled proteins and their co-receptors LRP5 and 6. The signal is then propagated to several downstream effectors, mediated by the phosphoprotein scaffold, dishevelled. We report a novel role ... ...

Abstract	Wnt signaling is initiated upon binding of Wnt proteins to Frizzled proteins and their co-receptors LRP5 and 6. The signal is then propagated to several downstream effectors, mediated by the phosphoprotein scaffold, dishevelled. We report a novel role for arginine methylation in regulating Wnt3a-stimulated LRP6 phosphorylation. G3BP2, a dishevelled-associated protein, is methylated in response to Wnt3a. The Wnt3a-induced LRP6 phosphorylation is attenuated by G3BP2 knockdown, chemical inhibition of methyl transferase activity or expression of methylation-deficient mutants of G3BP2. Arginine methylation of G3BP2 appears to be a Wnt3a-sensitive 'switch' regulating LRP6 phosphorylation and canonical Wnt-β-catenin signaling.
MeSH term(s)	Adaptor Proteins, Signal Transducing ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Arginine/metabolism ; Carrier Proteins/chemistry ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Line, Tumor ; Low Density Lipoprotein Receptor-Related Protein-6/genetics ; Low Density Lipoprotein Receptor-Related Protein-6/metabolism ; Methylation ; Mice ; Molecular Sequence Data ; Phosphorylation ; RNA-Binding Proteins ; Signal Transduction ; Up-Regulation ; Wnt3A Protein/genetics ; Wnt3A Protein/metabolism ; beta Catenin/metabolism ; ras GTPase-Activating Proteins/chemistry ; ras GTPase-Activating Proteins/genetics ; ras GTPase-Activating Proteins/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Carrier Proteins ; G3BP2 protein, human ; G3BP2 protein, mouse ; Low Density Lipoprotein Receptor-Related Protein-6 ; Lrp6 protein, mouse ; RNA-Binding Proteins ; Wnt3A Protein ; beta Catenin ; ras GTPase-Activating Proteins ; Arginine (94ZLA3W45F)
Language	English
Publishing date	2012-02-22
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.100933
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Article: G proteins in development.

Malbon, Craig C

Nature reviews. Molecular cell biology

2005 Volume 6, Issue 9, Page(s) 689–701

Abstract: ... adenylyl cyclases, phospholipase C and various ion channels. The convergence of developmental biology with cell ...

Abstract	The focus of developmental biologists has expanded from the analysis of gene expression to include the analysis of cell signalling. Heterotrimeric G proteins (G proteins) mediate signalling from a superfamily of heptahelical receptors (G-protein-coupled receptors) to a smaller number of effector units that include adenylyl cyclases, phospholipase C and various ion channels. The convergence of developmental biology with cell signalling has now revealed overlaps in which G proteins mediate complex pathways in embryonic development.
MeSH term(s)	Animals ; Developmental Biology ; GTP-Binding Proteins/metabolism ; Humans ; Models, Biological ; Morphogenesis/physiology ; Protein Subunits/metabolism ; Receptors, G-Protein-Coupled/metabolism ; Second Messenger Systems/physiology
Chemical Substances	Protein Subunits ; Receptors, G-Protein-Coupled ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2005-09
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	2031313-5
ISSN	1471-0080 ; 1471-0072
ISSN (online)	1471-0080
ISSN	1471-0072
DOI	10.1038/nrm1716
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Article ; Online: Beta-catenin, cancer, and G proteins: not just for frizzleds anymore.

Malbon, Craig C

Science's STKE : signal transduction knowledge environment

2005 Volume 2005, Issue 292, Page(s) pe35

Abstract: ... protein kinase C, and phosphorylation and inhibition of glycogen synthase kinase 3-beta. The phosphorylation ...

Abstract	The lipid metabolite lysophosphatidic acid (LPA) mediates an impressive set of responses that includes morphogenesis, cell proliferation, cell survival, cell adhesion, and cell migration. LPA exerts its downstream signaling by binding to the LPA(1), LPA(2), and LPA(3) (formerly Edg-2, -4, and -7) family of seven-transmembrane, segmented, heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors. LPA actions of therapeutic interest include effects on wound healing, atherogenesis, thrombogenesis, and, of course, cancer. LPA has been implicated in the progression of human breast, ovarian, prostate, head and neck, and colon malignancies. In view of these earlier observations, a recent report that LPA stimulates the proliferation of colon cancer-derived cell lines was greeted with great anticipation for its possible contribution to the unraveling of details of cancer signaling downstream of LPA. LPA was shown to stimulate nuclear accumulation of beta-catenin in a manner that depended on activation of Galpha(q) by LPA(2,3'), activation of phospholipase Cbeta, activation of a conventional protein kinase C, and phosphorylation and inhibition of glycogen synthase kinase 3-beta. The phosphorylation of beta-catenin by this kinase marks the protein for intracellular degradation; LPA suppresses this degradation and stimulates beta-catenin accumulation. Beta-catenin is a pivotal molecule in the control of cell cycle progression and gene expression, activating both processes in combination with lymphoid-enhancing factor/T cell-factor-sensitive transcription and inhibiting both processes in combination with FOXO transcription factors. The ability of LPA to increase the cytoplasmic and nuclear accumulation of beta-catenin provides a new dimension of knowledge linking lipid mediators to the dysregulation of beta-catenin signaling in cancer.
MeSH term(s)	Animals ; Cell Line, Tumor/drug effects ; Colonic Neoplasms/pathology ; Frizzled Receptors/chemistry ; Frizzled Receptors/physiology ; Heterotrimeric GTP-Binding Proteins/physiology ; Humans ; Invertebrates/physiology ; Isoenzymes/physiology ; JNK Mitogen-Activated Protein Kinases/physiology ; Lymphoid Enhancer-Binding Factor 1/physiology ; Lysophospholipids/pharmacology ; Lysophospholipids/physiology ; Models, Biological ; Neoplasm Proteins/chemistry ; Neoplasm Proteins/physiology ; Neoplasms/metabolism ; Phospholipase C beta ; Protein Kinase C/physiology ; Receptors, Lysophosphatidic Acid/drug effects ; Receptors, Lysophosphatidic Acid/physiology ; Signal Transduction ; Type C Phospholipases/physiology ; Vertebrates/physiology ; Wnt Proteins/physiology ; beta Catenin/physiology
Chemical Substances	Frizzled Receptors ; Isoenzymes ; Lymphoid Enhancer-Binding Factor 1 ; Lysophospholipids ; Neoplasm Proteins ; Receptors, Lysophosphatidic Acid ; Wnt Proteins ; beta Catenin ; Protein Kinase C (EC 2.7.11.13) ; JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Type C Phospholipases (EC 3.1.4.-) ; Phospholipase C beta (EC 3.1.4.11) ; Heterotrimeric GTP-Binding Proteins (EC 3.6.5.1) ; lysophosphatidic acid (PG6M3969SG)
Language	English
Publishing date	2005-07-12
Publishing country	United States
Document type	Journal Article ; Review
ISSN	1525-8882
ISSN (online)	1525-8882
DOI	10.1126/stke.2922005pe35
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Article ; Online: Probing the physical nature and composition of signalsomes.

Wang, Hsien-Yu / Malbon, Craig C

Journal of molecular signaling

2011 Volume 6, Issue 1, Page(s) 1

Abstract: Background: Recent advances in our understanding of cell signaling have revealed assemblies of signaling components often viewed in fluorescence microscopy as very large, irregular "punctae". These punctae are often dynamic in nature, appearing to act ... ...

Abstract	Background: Recent advances in our understanding of cell signaling have revealed assemblies of signaling components often viewed in fluorescence microscopy as very large, irregular "punctae". These punctae are often dynamic in nature, appearing to act as mobile scaffolds that function in integrating protein-protein interactions from large arrays of signaling components. The visualization of these punctae, termed "signalsomes" when applied to protein assemblies involved in cell signaling provokes the question, what is the physical nature of these structures made visible in live cells through the expression of fluorescently-tagged fusion molecules? Results: Steric-exclusion chromatography on wide-bore matrices, fluorescence correlation spectroscopy, and advanced proteomics permits the analysis of several important physical properties of signalsomes. Wnt canonical signaling is essential to normal cell development and dysregulation can lead to cancers in humans. Punctae/signalsomes have been reported based upon the study of fluorescently-tagged mammalian Dishevelleds. Dishevelleds are phosphoprotein scaffolds that demonstrate dynamic character and mobility in cells stimulated with Wnt3a. Recent studies have successfully isolated Dvl3-based signalsomes from mouse totipotent embryonic teratocarcinoma F9 cells in culture and sized by application of steric exclusion chromatography (SEC), displaying large discrete Mr (0.5 and 2 MDa). Activation of the Wnt canonical β-catenin/LEF-Tcf-sensitive transcriptional response leads to an upfield shift of >5 MDa of the Dvl3-based signalsome. Fluorescence correlation spectroscopy (fcs) is a single molecule analysis performed in live cells that experimentally measures the diffusion coefficient and permits calculation of MW of the signalsome (0.2 and 30 MDa species in vivo), which also reveal an upfield shift in MW in response to Wnt3a. Proteomics provides for molecular dissection of the composition of the signalsome isolated from untreated and Wnt3a-treated cells. Conclusion: Dvl3-based punctae/signalsomes made visible by fluorescent microscopy now can be interrogated by advanced physical means, defining such properties as signalsome Mr/MW, molecular composition, and intracellular locale.
Language	English
Publishing date	2011-01-11
Publishing country	England
Document type	Journal Article
ISSN	1750-2187
ISSN (online)	1750-2187
DOI	10.1186/1750-2187-6-1
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Article ; Online: Arginine methylation of G3BP1 in response to Wnt3a regulates β-catenin mRNA.

Bikkavilli, Rama Kamesh / Malbon, Craig C

Journal of cell science

2011 Volume 124, Issue Pt 13, Page(s) 2310–2320

Abstract: Wnt/β-catenin signaling is essential for normal mammalian development. Wnt3a activates the Wnt/β-catenin pathway through stabilization of β-catenin; a process in which the phosphoprotein Dishevelled figures prominently. Protein arginine methylation in ... ...

Abstract	Wnt/β-catenin signaling is essential for normal mammalian development. Wnt3a activates the Wnt/β-catenin pathway through stabilization of β-catenin; a process in which the phosphoprotein Dishevelled figures prominently. Protein arginine methylation in signaling complexes containing Dishevelled was investigated. Mass spectrometry of a prominent arginine-methylated, Dishevelled-associated protein identified the Ras GTPase activating protein-binding protein 1 G3BP1. Stimulation of totipotent mouse embryonic F9 cells with Wnt3a provoked increased methylation of G3BP1. We show that G3BP1 is a novel Ctnnb1 mRNA binding protein. Methylation of G3BP1 constitutes a molecular switch that regulates Ctnnb1 mRNA in response to Wnt3a. Thus, the protein arginine methylation that targets G3BP1 acts as a novel regulator of Ctnnb1 mRNA.
MeSH term(s)	Adaptor Proteins, Signal Transducing ; Animals ; Arginine/metabolism ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Line, Tumor ; DNA Helicases ; Dishevelled Proteins ; Methylation ; Mice ; Phosphoproteins ; Poly-ADP-Ribose Binding Proteins ; RNA Helicases ; RNA Recognition Motif Proteins ; RNA, Messenger/metabolism ; RNA-Binding Proteins ; Signal Transduction ; Wnt3A Protein/genetics ; Wnt3A Protein/metabolism ; beta Catenin/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; CTNNB1 protein, mouse ; Carrier Proteins ; Dishevelled Proteins ; Phosphoproteins ; Poly-ADP-Ribose Binding Proteins ; RNA Recognition Motif Proteins ; RNA, Messenger ; RNA-Binding Proteins ; Wnt3A Protein ; Wnt3a protein, mouse ; beta Catenin ; Arginine (94ZLA3W45F) ; DNA Helicases (EC 3.6.4.-) ; G3bp1 protein, mouse (EC 3.6.4.12) ; RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2011-06-07
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.084046
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Article ; Online: Insulin signalling: putting the 'G-' in protein-protein interactions.

Malbon, Craig C

The Biochemical journal

2004 Volume 380, Issue Pt 3, Page(s) e11–2

Abstract: Cell signalling via receptor tyrosine kinases, such as the insulin receptor, and via heterotrimeric G-proteins, such as Galpha(i), Galpha(s) and Galpha(q) family members, constitute two of most avidly studied paradigms in cell biology. That elements of ... ...

Abstract	Cell signalling via receptor tyrosine kinases, such as the insulin receptor, and via heterotrimeric G-proteins, such as Galpha(i), Galpha(s) and Galpha(q) family members, constitute two of most avidly studied paradigms in cell biology. That elements of these two populous signalling pathways must cross-talk to achieve proper signalling in the regulation of cell proliferation, differentiation and metabolism has been anticipated, but the evolution of our thinking and the analysis of such cross-talk have lagged behind the ever-expanding troupe of players and the recognition of multivalency as the rule, rather than the exception, in signalling biology. New insights have been provided by Kreuzer et al. in this issue of the Biochemical Journal, in which insulin is shown to provoke recruitment of Galpha(i)-proteins to insulin-receptor-based complexes that can regulate the gain of insulin-receptor-catalysed autophosphorylation, a proximal point in the insulin-sensitive cascade of signalling. Understanding the convergence and cross-talk of signals from the receptor tyrosine kinases and G-protein-coupled receptor pathways in physical, spatial and temporal contexts will remain a major challenge of cell biology.
MeSH term(s)	Animals ; Heterotrimeric GTP-Binding Proteins/metabolism ; Humans ; Insulin/metabolism ; Protein Interaction Mapping/methods ; Receptor, Insulin/metabolism ; Signal Transduction/physiology
Chemical Substances	Insulin ; Receptor, Insulin (EC 2.7.10.1) ; Heterotrimeric GTP-Binding Proteins (EC 3.6.5.1)
Language	English
Publishing date	2004-06-15
Publishing country	England
Document type	Comment ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BJ20040619
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Article: Frizzleds: new members of the superfamily of G-protein-coupled receptors.

Malbon, Craig C

Frontiers in bioscience : a journal and virtual library

2004 Volume 9, Page(s) 1048–1058

Abstract: The superfamily of membrane receptors that signal via heterotrimeric G-proteins includes more than 1500 members, classified into five basic groups, representing about 5-10% of the human genome. These G-protein-coupled receptors operate through a ... ...

Abstract	The superfamily of membrane receptors that signal via heterotrimeric G-proteins includes more than 1500 members, classified into five basic groups, representing about 5-10% of the human genome. These G-protein-coupled receptors operate through a comparatively smaller group of heterotrimeric G-protein family of approximately 20 members, each displaying an alpha subunit that binds and hydrolyzes GTP in combination with the beta-/gamma-subunit complex that is largely non-dissociable in vivo. Frizzleds represent the cell membrane receptors for a family of secreted glycoprotein ligands termed "Wnts" that play essential roles in development, including cell fate, adhesion, polarity, migration, and proliferation. Based upon a compelling set of experimental observations about the structure and downstream signaling of Wnt-Frizzled signaling, one can only conclude that Frizzleds are true members of the GPCR family and require heterotrimeric G-proteins to propagate signals from the Wnts to well-known effectors, including beta-catenin stabilization, mobilization of intracellular Ca2+, and activation of cyclic GMP phosphodiesterase. Careful study of primary structure of Frizzleds reveal heptihelical, 7-transmembrane segments, characteristic of GPCRs. Chimeric forms of Frizzleds, making use of the cytoplasmic domains of Frizzleds, substituted into the exofacial and transmembrane segments of the prototypic GPCR beta2-adrenergic receptor are functional and display the well-known GTP-shift in receptor affinity. Suppression of specific G-protein subunits suppress the ability of chimeric as well as authentic Frizzled-1 and Frizzled-2 to signal to their canonical pathways upon activation. The involvement of beta-arrestin, an important regulator of GPCR signaling, in Frizzled signaling is, therefore, not unexpected. Recognition of the GPCR character of Frizzled enables a more broad understanding of these receptors and of their mechanisms of downstream signaling.
MeSH term(s)	Animals ; Frizzled Receptors ; Proteins/chemistry ; Proteins/classification ; Proteins/physiology ; Proto-Oncogene Proteins/physiology ; Receptors, G-Protein-Coupled/chemistry ; Receptors, G-Protein-Coupled/classification ; Receptors, G-Protein-Coupled/physiology ; Receptors, Neurotransmitter/physiology ; Signal Transduction ; Wnt Proteins ; Zebrafish Proteins
Chemical Substances	FZD1 protein, human ; FZD2 protein, human ; Frizzled Receptors ; Proteins ; Proto-Oncogene Proteins ; Receptors, G-Protein-Coupled ; Receptors, Neurotransmitter ; Wnt Proteins ; Zebrafish Proteins
Language	English
Publishing date	2004-05-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	2141320-4
ISSN	1093-9946
ISSN	1093-9946
DOI	10.2741/1308
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Article ; Online: Dishevelled-KSRP complex regulates Wnt signaling through post-transcriptional stabilization of beta-catenin mRNA.

Bikkavilli, Rama Kamesh / Malbon, Craig C

Journal of cell science

2010 Volume 123, Issue Pt 8, Page(s) 1352–1362

Abstract: Canonical Wnt/beta-catenin signaling is crucial during embryonic development. Upon Wnt stimulation, Dishevelled proteins relay the signal from upstream Frizzled receptors to downstream effectors. By using affinity purification followed by ion-trap mass ... ...

Abstract	Canonical Wnt/beta-catenin signaling is crucial during embryonic development. Upon Wnt stimulation, Dishevelled proteins relay the signal from upstream Frizzled receptors to downstream effectors. By using affinity purification followed by ion-trap mass spectrometry we identified K-homology splicing regulator protein (KSRP) as a novel Dishevelled-interacting protein. We show that KSRP negatively regulates Wnt/beta-catenin signaling at the level of post-transcriptional CTNNB1 (beta-catenin) mRNA stability. Thus, Dishevelled-KSRP complex operates in Wnt regulation of beta-catenin, functioning post-transcriptionally upon CTNNB1 mRNA stability.
MeSH term(s)	Adaptor Proteins, Signal Transducing/chemistry ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Cell Line ; Colonic Neoplasms/metabolism ; Colonic Neoplasms/pathology ; Dishevelled Proteins ; Half-Life ; Mass Spectrometry ; Mice ; Models, Biological ; Phosphoproteins/chemistry ; Phosphoproteins/metabolism ; Protein Binding/drug effects ; Protein Structure, Tertiary ; RNA Processing, Post-Transcriptional/drug effects ; RNA Stability/drug effects ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/metabolism ; Signal Transduction/drug effects ; Trans-Activators/chemistry ; Trans-Activators/metabolism ; Wnt Proteins/metabolism ; Wnt Proteins/pharmacology ; Wnt3 Protein ; beta Catenin/genetics ; beta Catenin/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Dishevelled Proteins ; KHSRP protein, human ; KSRP protein, mouse ; Phosphoproteins ; RNA, Messenger ; RNA-Binding Proteins ; Trans-Activators ; Wnt Proteins ; Wnt3 Protein ; beta Catenin
Language	English
Publishing date	2010-03-23
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.056176
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