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  • 1
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    Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-10-13
    Description: The PKB (protein kinase B, also called Akt) family of protein kinases plays a key role in insulin signaling, cellular survival, and transformation. PKB is activated by phosphorylation on residues threonine 308, by the protein kinase PDK1, and Serine 473, by a putative serine 473 kinase. Several protein binding partners for PKB have been identified. Here, we describe a protein partner for PKBalpha termed CTMP, or carboxyl-terminal modulator protein, that binds specifically to the carboxyl-terminal regulatory domain of PKBalpha at the plasma membrane. Binding of CTMP reduces the activity of PKBalpha by inhibiting phosphorylation on serine 473 and threonine 308. Moreover, CTMP expression reverts the phenotype of v-Akt-transformed cells examined under a number of criteria including cell morphology, growth rate, and in vivo tumorigenesis. These findings identify CTMP as a negative regulatory component of the pathway controlling PKB activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maira, S M -- Galetic, I -- Brazil, D P -- Kaech, S -- Ingley, E -- Thelen, M -- Hemmings, B A -- New York, N.Y. -- Science. 2001 Oct 12;294(5541):374-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher Institute, Post Office Box 2543, CH-4002 Basel, Switzerland., Institute for Research in Biomedicine, CH-6500 Bellinzona, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11598301" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Division ; Cell Line ; Cell Line, Transformed ; Cell Membrane/*metabolism ; Cell Size ; Enzyme Activation ; Genes, fos ; Humans ; Insulin/pharmacology ; Insulin-Like Growth Factor I/pharmacology ; Membrane Proteins/chemistry/genetics/*metabolism ; Mice ; Mice, Nude ; Molecular Sequence Data ; Neoplasms, Experimental/etiology ; Oncogene Protein v-akt ; Phosphorylation ; Promoter Regions, Genetic ; Protein Binding ; Protein-Serine-Threonine Kinases/*metabolism ; *Proto-Oncogene Proteins ; Proto-Oncogene Proteins c-akt ; Recombinant Fusion Proteins/metabolism ; Retroviridae Proteins, Oncogenic/genetics/*metabolism ; Signal Transduction ; Thiolester Hydrolases ; Transcription, Genetic ; Transfection ; Tumor Cells, Cultured ; Vanadates/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    PH domains--a universal membrane adapter (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hemmings, B A -- New York, N.Y. -- Science. 1997 Mar 28;275(5308):1899.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher Institute, Post Office Box 2543, Basel, Switzerland. hemmings@fmi.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9122692" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Proteins/*chemistry ; Cell Adhesion Molecules/metabolism ; Cell Membrane/*metabolism ; GTP-Binding Proteins/metabolism ; *GTPase-Activating Proteins ; Guanine Nucleotide Exchange Factors ; Inositol Phosphates/metabolism ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositol Phosphates/metabolism ; *Phosphoproteins ; Phosphotransferases (Alcohol Group Acceptor)/chemistry/*metabolism ; Proteins/metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism ; Second Messenger Systems ; *Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Akt signaling: linking membrane events to life and death decisions (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hemmings, B A -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):628-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher Institute, Post Office Box 2543, CH-4002, Basel, Switzerland. hemmings@fmi.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9019819" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Cell Membrane/*metabolism ; Enzyme Activation ; Growth Substances/pharmacology ; Neurons/*cytology/metabolism ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositol Phosphates/metabolism ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; *Protein-Serine-Threonine Kinases ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-akt ; Second Messenger Systems ; *Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Phosphorylation and activation of p70s6k by PDK1 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-21
    Description: Activation of the protein p70s6k by mitogens leads to increased translation of a family of messenger RNAs that encode essential components of the protein synthetic apparatus. Activation of the kinase requires hierarchical phosphorylation at multiple sites, culminating in the phosphorylation of the threonine in position 229 (Thr229), in the catalytic domain. The homologous site in protein kinase B (PKB), Thr308, has been shown to be phosphorylated by the phosphoinositide-dependent protein kinase PDK1. A regulatory link between p70s6k and PKB was demonstrated, as PDK1 was found to selectively phosphorylate p70s6k at Thr229. More importantly, PDK1 activated p70s6k in vitro and in vivo, whereas the catalytically inactive PDK1 blocked insulin-induced activation of p70s6k.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pullen, N -- Dennis, P B -- Andjelkovic, M -- Dufner, A -- Kozma, S C -- Hemmings, B A -- Thomas, G -- New York, N.Y. -- Science. 1998 Jan 30;279(5351):707-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher Institute, Maulbeerstrasse 66, CH-4058, Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9445476" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Phosphoinositide-Dependent Protein Kinases ; Amino Acid Sequence ; Androstadienes/pharmacology ; Animals ; Binding Sites ; Calcium-Calmodulin-Dependent Protein Kinase Type 4 ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Catalysis ; Cell Line ; Enzyme Activation ; Insulin/pharmacology ; Insulin Antagonists/pharmacology ; Molecular Sequence Data ; Phosphorylation ; Phosphothreonine/metabolism ; Polyenes/pharmacology ; Protein-Serine-Threonine Kinases/*metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Recombinant Proteins/metabolism ; Ribosomal Protein S6 Kinases/*metabolism ; Sirolimus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    Living with lethal PIP3 levels: viability of flies lacking PTEN restored by a PH domain mutation in Akt/PKB (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-02
    Description: The phosphoinositide phosphatase PTEN is mutated in many human cancers. Although the role of PTEN has been studied extensively, the relative contributions of its numerous potential downstream effectors to deregulated growth and tumorigenesis remain uncertain. We provide genetic evidence in Drosophila melanogaster for the paramount importance of the protein kinase Akt [also called protein kinase B (PKB)] in mediating the effects of increased phosphatidylinositol 3,4,5-trisphosphate (PIP3) concentrations that are caused by the loss of PTEN function. A mutation in the pleckstrin homology (PH) domain of Akt that reduces its affinity for PIP3 sufficed to rescue the lethality of flies devoid of PTEN activity. Thus, Akt appears to be the only critical target activated by increased PIP3 concentrations in Drosophila.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stocker, Hugo -- Andjelkovic, Mirjana -- Oldham, Sean -- Laffargue, Muriel -- Wymann, Matthias P -- Hemmings, Brian A -- Hafen, Ernst -- New York, N.Y. -- Science. 2002 Mar 15;295(5562):2088-91. Epub 2002 Feb 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoologisches Institut der Universitat Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872800" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Substitution ; Animals ; Cell Line ; Cell Membrane/enzymology ; Drosophila Proteins/chemistry/genetics/metabolism ; Drosophila melanogaster/genetics/*physiology ; Eye/growth & development ; Female ; Genes, Insect ; Humans ; Insulin/pharmacology ; Male ; Mutation ; PTEN Phosphohydrolase ; Phenotype ; Phosphatidylinositol 4,5-Diphosphate/metabolism ; Phosphatidylinositol Phosphates/*metabolism ; Phosphoric Monoester Hydrolases/*genetics/*physiology ; Photoreceptor Cells, Invertebrate/growth & development ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/chemistry/*genetics/metabolism ; Proto-Oncogene Proteins/chemistry/*genetics/metabolism ; Proto-Oncogene Proteins c-akt ; Transfection ; Tumor Suppressor Proteins/*genetics/*physiology ; Vanadates/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 6
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    Cell signaling. Blocking Akt-ivity (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Restuccia, David F -- Hemmings, Brian A -- New York, N.Y. -- Science. 2009 Aug 28;325(5944):1083-4. doi: 10.1126/science.1179972.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058 Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19713516" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Antineoplastic Agents/therapeutic use ; Apoptosis ; Cell Line, Tumor ; Cell Membrane/metabolism ; Enzyme Activation ; Humans ; Mice ; Mice, Nude ; Mutation ; Neoplasms/drug therapy/*metabolism/pathology ; Protein Transport ; Proto-Oncogene Proteins c-akt/chemistry/genetics/*metabolism ; RNA Interference ; *Signal Transduction ; Sirolimus/analogs & derivatives/therapeutic use ; TNF Receptor-Associated Factor 6/antagonists & inhibitors/genetics/*metabolism ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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