Mutations in v-Src SH3 and catalytic domains that jointly confer temperature-sensitive transformation with minimal temperature-dependent changes in cellular tyrosine phosphorylation

No abstract is available for this paper.

• Publication year

  1994

• Venue

  Journal of Virology

• Publication date

  1994-07-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1128/jvi.68.7.4392-4399.1994PMID 8207813PMCID PMC236363
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Highly conserved amino acids in the SH2 and catalytic domains of v-src are altered in naturally occurring, transformation-defective alleles.

  1994cited by this paper
• SH2 and SH3 domains.

  1993cited by this paper
• Closing in on SH2 specificity.

  1993cited by this paper
• Deletion of the SH3 domain of Src interferes with regulation by the phosphorylated carboxyl-terminal tyrosine.

  1993cited by this paper
• The v-Src SH3 domain binds phosphatidylinositol 3'-kinase

  1993cited by this paper
• Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides

  1993cited by this paper
• Csk inhibition of c‐Src activity requires both the SH2 and SH3 domains of Src.

  1993cited by this paper
• Signalling through SH2 and SH3 domains.

  1993cited by this paper
• Small deletion in v-src SH3 domain of a transformation defective mutant of Rous sarcoma virus restores wild type transforming properties.

  1992cited by this paper
• SH2 and SH3 domains: from structure to function.

  1992cited by this paper
• Mutations in the SH3 domain of the src oncogene which decrease association of phosphatidylinositol 3'-kinase activity with pp60v-src and alter cellular morphology

  1992influential reference
• Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src

  1992cited by this paper
• Solution structure of the SH3 domain of Src and identification of its ligand-binding site.

  1992cited by this paper
• The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110.

  1991cited by this paper
• Mitogenesis induced by pp60v-src is not accompanied by increased expression of immediate early response genes.

  1990cited by this paper
• Association of the v-crk oncogene product with phosphotyrosine-containing proteins and protein kinase activity.

  1990cited by this paper
• Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src

  1990cited by this paper
• Mutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells.

  1990cited by this paper
• The amino-terminal region of pp60c-src has a modulatory role and contains multiple sites of tyrosine phosphorylation.

  1990cited by this paper
• Linker insertion-deletion mutagenesis of the v-src gene: isolation of host- and temperature-dependent mutants

  1989cited by this paper
• Construction of mutant and chimeric genes using the polymerase chain reaction.

  1989cited by this paper
• Activation of pp60c-src transforming potential by mutations altering the structure of an amino terminal domain containing residues 90-95.

  1988cited by this paper
• A single point mutation has pleiotropic effects on pp60v-src function

  1988cited by this paper
• Genetic analysis of the form and function of the viral src oncogene product.

  1987cited by this paper
• Molecular cloning of the intronless EJ ras oncogene using a murine retrovirus shuttle vector

  1986cited by this paper
• Amino acid substitutions sufficient to convert the nontransforming p60c-src protein to a transforming protein

  1986cited by this paper
• Localization of temperature-sensitive transformation mutations and back mutations in the Rous sarcoma virus src gene

  1986cited by this paper
• The use of Rous sarcoma virus transformation mutants with differing tyrosine kinase activities to study the relationships between vinculin phosphorylation, pp60v-src location and adhesion plaque integrity.

  1986cited by this paper
• Neither arginine nor histidine can carry out the function of lysine-295 in the ATP-binding site of p60src

  1986cited by this paper
• Genetic analysis of p60v-src domains involved in the induction of different cell transformation parameters

  1986cited by this paper
• Genetic lesions involved in temperature sensitivity of the src gene products of four Rous sarcoma virus mutants

  1986cited by this paper
• Intracellular localization and processing of pp60v-src proteins expressed by two distinct temperature-sensitive mutants of Rous sarcoma virus

  1986cited by this paper
• A mutation at the ATP-binding site of pp60v-src abolishes kinase activity, transformation, and tumorigenicity

  1985cited by this paper
• Functional domains of the pp60v-src protein as revealed by analysis of temperature-sensitive Rous sarcoma virus mutants

  1984cited by this paper
• Detection and quantification of phosphotyrosine in proteins.

  1983cited by this paper
• Molecular cloning of the avian erythroblastosis virus genome and recovery of oncogenic virus by transfection of chicken cells

  1980cited by this paper
• A mutant of Rous sarcoma virus with a thermolabile defect in the virus envelope.

  1978cited by this paper
• Temperature-sensitive avian sarcoma viruses: a physiological comparison of twenty mutants.

  1973cited by this paper

• Disulfide Bridging the Gap between Src and Cortactin: A New Paradigm in SH2 Domain-mediated Signaling

  2013cites this paper
• Tyrosine Phosphorylation of Missing in Metastasis Protein Is Implicated in Platelet-derived Growth Factor-mediated Cell Shape Changes*

  2007cites this paper
• The SH4-Unique-SH3-SH2 domains dictate specificity in signaling that differentiate c-Yes from c-Src

  2003cites this paper
• The case for high-dose adjuvant chemotherapy in breast cancer: (II) clinical experience

  2002cites this paper
• TheRoleoftheSrcHomology Domainsin Morphological Transformation byv-src

  1997cites this paper
• Distinctive regulation of v-Src-associated phosphatidylinositol 3-kinase during PC12 cell differentiation.

  1997cites this paper
• The role of the Src homology domains in morphological transformation by v-src.

  1997cites this paper
• Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins

  1996cites this paper
• v-Src induces constitutive macropinocytosis in rat fibroblasts.

  1996cites this paper
• The case for high-dose adjuvant chemotherapy in breast cancer: (II) clinical experience.

  1996cites this paper
• Cooperation of Src Homology Domains in the Regulated Binding of Phosphatidylinositol 3-Kinase

  1995cites this paper
• An amino acid substitution in the Drosophila hopTum‐l Jak kinase causes leukemia‐like hematopoietic defects.

  1995cites this paper
• v-Src-induced degradation of focal adhesion kinase during morphological transformation of chicken embryo fibroblasts.

  1995cites this paper
• A Bcl‐2‐related gene is activated in avian cells transformed by the Rous sarcoma virus.

  1995cites this paper
• Functions of the v‐SRC protein tyrosine kinase

  1994cites this paper