NDLI: In vivo binding properties of SH2 domains from GTPase-activating protein and phosphatidylinositol 3-kinase.

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The human prointerleukin 1 beta gene requires DNA sequences both proximal and distal to the transcription start site for tissue-specific induction.

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V(D)J recombination: signal and coding joint resolution are uncoupled and depend on parallel synapsis of the sites.

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Regulated splicing of the Drosophila sex-lethal male exon involves a blockage mechanism.

p53-mediated cell death: relationship to cell cycle control.

Identification of a pentanucleotide telomeric sequence, (TTAGG)n, in the silkworm Bombyx mori and in other insects.

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SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange.

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Ligand-dependent, Pit-1/growth hormone factor-1 (GHF-1)-independent transcriptional stimulation of rat growth hormone gene expression by thyroid hormone receptors in vitro.

In vivo binding properties of SH2 domains from GTPase-activating protein and phosphatidylinositol 3-kinase.

Purification and characterization of the stage-specific embryonic enhancer-binding protein SSAP-1.

Progression of interleukin-2 (IL-2)-dependent rat T cell lymphoma lines to IL-2-independent growth following activation of a gene (Gfi-1) encoding a novel zinc finger protein.

Differential pp40I kappa B-beta inhibition of DNA binding by rel proteins.

A dosage-dependent suppressor of a temperature-sensitive calmodulin mutant encodes a protein related to the fork head family of DNA-binding proteins.

Inactivation of erythropoietin receptor function by point mutations in a region having homology with other cytokine receptors.

A mitogen-responsive promoter region that is synergistically activated through multiple signalling pathways.

Transcriptional repression in Saccharomyces cerevisiae by a SIN3-LexA fusion protein.

cis regulation of the keratin 18 gene in transgenic mice.

Alpha B-crystallin expression in mouse NIH 3T3 fibroblasts: glucocorticoid responsiveness and involvement in thermal protection.

COUP-TF acts as a competitive repressor for estrogen receptor-mediated activation of the mouse lactoferrin gene.

Downregulation of Ke 6, a novel gene encoded within the major histocompatibility complex, in murine polycystic kidney disease.

A nuclear factor for interleukin-6 expression (NF-IL6) and the glucocorticoid receptor synergistically activate transcription of the rat alpha 1-acid glycoprotein gene via direct protein-protein interaction.

Redistribution of activated pp60c-src to integrin-dependent cytoskeletal complexes in thrombin-stimulated platelets.

Near-zero linking difference upon transcription factor IID binding to promoter DNA.

PRP19: a novel spliceosomal component.

The yeast PRP19 protein is not tightly associated with small nuclear RNAs, but appears to associate with the spliceosome after binding of U2 to the pre-mRNA and prior to formation of the functional spliceosome.

Nonsense codons can reduce the abundance of nuclear mRNA without affecting the abundance of pre-mRNA or the half-life of cytoplasmic mRNA.

Epidermal growth factor regulates the exchange rate of guanine nucleotides on p21ras in fibroblasts.

The NFAT-1 DNA binding complex in activated T cells contains Fra-1 and JunB.

Evidence that GCD6 and GCD7, translational regulators of GCN4, are subunits of the guanine nucleotide exchange factor for eIF-2 in Saccharomyces cerevisiae.

Kid-1, a putative renal transcription factor: regulation during ontogeny and in response to ischemia and toxic injury.

Extinction of T cell receptor alpha-chain gene expression accompanied by loss of the lymphoid enhancer-binding factor 1 (LEF-1) in murine somatic cell hybrids.

A human mitochondrial transcriptional activator can functionally replace a yeast mitochondrial HMG-box protein both in vivo and in vitro.

The alpha-mating type locus of Cryptococcus neoformans contains a peptide pheromone gene.

Selective destabilization of short-lived mRNAs with the granulocyte-macrophage colony-stimulating factor AU-rich 3' noncoding region is mediated by a cotranslational mechanism.

The EBNA2-Related Resistance Towards Alpha Interferon (IFN-α) in Burkitt's Lymphoma Cells Effects Induction of IFN-Induced Genes but Not the Activation of Transcription Factor ISGF-3

A Common Intermediary Factor (p52/54) Recognizing “Acidic Blob”-Type Domains Is Required for Transcriptional Activation by the Jun Proteins

The Plant Amino Acid Mimosine May Inhibit Initiation at Origins of Replication in Chinese Hamster Cells

P Nucleotides in V(D)J Recombination: A Fine-Structure Analysis

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In vivo binding properties of SH2 domains from GTPase-activating protein and phosphatidylinositol 3-kinase.

Content Provider	PubMed Central
Author	Cooper, J. A. Kashishian, A.
Abstract	We have used a transient expression system and mutant platelet-derived growth factor (PDGF) receptors to study the binding specificities of the Src homology 2 (SH2) regions of the Ras GTPase-activator protein (GAP) and the p85 alpha subunit of phosphatidylinositol 3-kinase (PI3 kinase). A number of fusion proteins, each tagged with an epitope allowing recognition by a monoclonal antibody, were expressed at levels comparable to those of endogenous GAP. Fusion proteins containing the central SH2-SH3-SH2 region of GAP or the C-terminal region of p85 alpha, which includes two SH2 domains, bound to PDGF receptors in response to PDGF stimulation. Both fusion proteins showed the same requirements for tyrosine phosphorylation sites in the PDGF receptor as the full-length proteins from which they were derived, i.e., binding of the GAP fusion protein was reduced by mutation of Tyr-771, and binding of the p85 fusion protein was reduced by mutation of Tyr-740, Tyr-751, or both residues. Fusion proteins containing single SH2 domains from either GAP or p85 alpha did not bind detectably to PDGF receptors in this system, suggesting that two SH2 domains in a single polypeptide cooperate to raise the affinity of binding. The sequence specificities of individual SH2 domains were deduced from the binding properties of fusion proteins containing one SH2 domain from GAP and another from p85. The results suggest that the C-terminal GAP SH2 domain specifies binding to Tyr-771, the C-terminal p85 alpha SH2 domain binds to either Tyr-740 or Tyr-751, and each protein's N-terminal SH2 domain binds to unidentified phosphorylation sites.(ABSTRACT TRUNCATED AT 250 WORDS)
Starting Page	1737
File Format	PDF
ISSN	10985549
e-ISSN	10985549
Journal	Molecular and Cellular Biology
Issue Number	3
Volume Number	13
Language	English
Publisher Date	1993-03-01
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology

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