Matches in SemOpenAlex for { <https://semopenalex.org/work/W2041940006> ?p ?o ?g. }
Showing items 1 to 96 of
96
with 100 items per page.
- W2041940006 endingPage "5599" @default.
- W2041940006 startingPage "5594" @default.
- W2041940006 abstract "The LIM domain protein rhombotin-2 (RBTN-2/TTG-2/LMO2) is involved in many processes, including leukemogenesis and erythropoiesis. It is thought that the principle role of RBTN-2 in these processes is to regulate transcription. To examine the potential for RBTN-2 to modulate transcription, we constructed RBTN-2/GAL4 DNA-binding domain fusion proteins and measured their ability to activate transcription of a reporter gene construct. From these studies we identified a transcription activation domain within the NH2 terminus of RBTN-2. This activation domain was further localized within a proline-rich 19-amino acid region. A second activation domain of 11 amino acids was also identified. This domain was located within the COOH terminus of RBTN-2, and functioned in mammalian cells but not in yeast. Furthermore, the two LIM domains of RBTN-2 were shown to function as transcription repression domains. Each individual LIM domain acted as an independent transcription repression domain on a heterologous activation domain. However, in context of full-length RBTN-2, the LIM domains selectively repressed the NH2-terminal activation domain, but had no effect on the COOH-terminal domain. Overall, these results demonstrate that the T-cell oncogene RBTN-2 is a complex transcription factor possessing multiple transcription regulatory modules, including two activation domains and two repression domains. The LIM domain protein rhombotin-2 (RBTN-2/TTG-2/LMO2) is involved in many processes, including leukemogenesis and erythropoiesis. It is thought that the principle role of RBTN-2 in these processes is to regulate transcription. To examine the potential for RBTN-2 to modulate transcription, we constructed RBTN-2/GAL4 DNA-binding domain fusion proteins and measured their ability to activate transcription of a reporter gene construct. From these studies we identified a transcription activation domain within the NH2 terminus of RBTN-2. This activation domain was further localized within a proline-rich 19-amino acid region. A second activation domain of 11 amino acids was also identified. This domain was located within the COOH terminus of RBTN-2, and functioned in mammalian cells but not in yeast. Furthermore, the two LIM domains of RBTN-2 were shown to function as transcription repression domains. Each individual LIM domain acted as an independent transcription repression domain on a heterologous activation domain. However, in context of full-length RBTN-2, the LIM domains selectively repressed the NH2-terminal activation domain, but had no effect on the COOH-terminal domain. Overall, these results demonstrate that the T-cell oncogene RBTN-2 is a complex transcription factor possessing multiple transcription regulatory modules, including two activation domains and two repression domains." @default.
- W2041940006 created "2016-06-24" @default.
- W2041940006 creator A5006819204 @default.
- W2041940006 creator A5017494299 @default.
- W2041940006 creator A5080789872 @default.
- W2041940006 date "1997-02-01" @default.
- W2041940006 modified "2023-10-12" @default.
- W2041940006 title "T-cell Proto-oncogene Rhombotin-2 Is a Complex Transcription Regulator Containing Multiple Activation and Repression Domains" @default.
- W2041940006 cites W1232714476 @default.
- W2041940006 cites W1669280308 @default.
- W2041940006 cites W1756418163 @default.
- W2041940006 cites W1958059146 @default.
- W2041940006 cites W1966018982 @default.
- W2041940006 cites W1972766406 @default.
- W2041940006 cites W1979800592 @default.
- W2041940006 cites W1982756681 @default.
- W2041940006 cites W1989274470 @default.
- W2041940006 cites W1989429141 @default.
- W2041940006 cites W1992178795 @default.
- W2041940006 cites W1996121905 @default.
- W2041940006 cites W2006136518 @default.
- W2041940006 cites W2022339270 @default.
- W2041940006 cites W2022668368 @default.
- W2041940006 cites W2026688799 @default.
- W2041940006 cites W2032881439 @default.
- W2041940006 cites W2050018959 @default.
- W2041940006 cites W2051296872 @default.
- W2041940006 cites W2056328047 @default.
- W2041940006 cites W2071517621 @default.
- W2041940006 cites W2089218510 @default.
- W2041940006 cites W2138304761 @default.
- W2041940006 cites W2142946131 @default.
- W2041940006 cites W2146198196 @default.
- W2041940006 cites W2147561347 @default.
- W2041940006 cites W2346876622 @default.
- W2041940006 cites W2415586388 @default.
- W2041940006 cites W256290002 @default.
- W2041940006 cites W25692858 @default.
- W2041940006 doi "https://doi.org/10.1074/jbc.272.9.5594" @default.
- W2041940006 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9038167" @default.
- W2041940006 hasPublicationYear "1997" @default.
- W2041940006 type Work @default.
- W2041940006 sameAs 2041940006 @default.
- W2041940006 citedByCount "16" @default.
- W2041940006 crossrefType "journal-article" @default.
- W2041940006 hasAuthorship W2041940006A5006819204 @default.
- W2041940006 hasAuthorship W2041940006A5017494299 @default.
- W2041940006 hasAuthorship W2041940006A5080789872 @default.
- W2041940006 hasBestOaLocation W20419400061 @default.
- W2041940006 hasConcept C104317684 @default.
- W2041940006 hasConcept C10522644 @default.
- W2041940006 hasConcept C138885662 @default.
- W2041940006 hasConcept C144292202 @default.
- W2041940006 hasConcept C150194340 @default.
- W2041940006 hasConcept C179926584 @default.
- W2041940006 hasConcept C186310378 @default.
- W2041940006 hasConcept C33987129 @default.
- W2041940006 hasConcept C41895202 @default.
- W2041940006 hasConcept C54355233 @default.
- W2041940006 hasConcept C86339819 @default.
- W2041940006 hasConcept C86803240 @default.
- W2041940006 hasConcept C95444343 @default.
- W2041940006 hasConceptScore W2041940006C104317684 @default.
- W2041940006 hasConceptScore W2041940006C10522644 @default.
- W2041940006 hasConceptScore W2041940006C138885662 @default.
- W2041940006 hasConceptScore W2041940006C144292202 @default.
- W2041940006 hasConceptScore W2041940006C150194340 @default.
- W2041940006 hasConceptScore W2041940006C179926584 @default.
- W2041940006 hasConceptScore W2041940006C186310378 @default.
- W2041940006 hasConceptScore W2041940006C33987129 @default.
- W2041940006 hasConceptScore W2041940006C41895202 @default.
- W2041940006 hasConceptScore W2041940006C54355233 @default.
- W2041940006 hasConceptScore W2041940006C86339819 @default.
- W2041940006 hasConceptScore W2041940006C86803240 @default.
- W2041940006 hasConceptScore W2041940006C95444343 @default.
- W2041940006 hasIssue "9" @default.
- W2041940006 hasLocation W20419400061 @default.
- W2041940006 hasOpenAccess W2041940006 @default.
- W2041940006 hasPrimaryLocation W20419400061 @default.
- W2041940006 hasRelatedWork W1588590203 @default.
- W2041940006 hasRelatedWork W1986853146 @default.
- W2041940006 hasRelatedWork W2003154348 @default.
- W2041940006 hasRelatedWork W2003398557 @default.
- W2041940006 hasRelatedWork W2032552404 @default.
- W2041940006 hasRelatedWork W2102749197 @default.
- W2041940006 hasRelatedWork W2107038109 @default.
- W2041940006 hasRelatedWork W2370952936 @default.
- W2041940006 hasRelatedWork W2789700864 @default.
- W2041940006 hasRelatedWork W4251719759 @default.
- W2041940006 hasVolume "272" @default.
- W2041940006 isParatext "false" @default.
- W2041940006 isRetracted "false" @default.
- W2041940006 magId "2041940006" @default.
- W2041940006 workType "article" @default.