The Single Transmembrane Domains of Human Receptor Tyrosine Kinases Encode Self-Interactions
- Publication type:
- Journal article
- Metadata:
-
- Abstract
- <jats:p>The transmembrane domain of any of the 58 human receptor tyrosine kinases is sufficient to mediate dimerization.</jats:p>
- Autoren
- Carmen Finger
- Claudia Escher
- Dirk Schneider
- DOI
- 10.1126/scisignal.2000547
- eISSN
- 1937-9145
- ISSN
- 1945-0877
- Ausgabe der Veröffentlichung
- 89
- Zeitschrift
- Science Signaling
- Sprache
- en
- Datum der Veröffentlichung
- 2009
- Status
- Published
- Herausgeber
- American Association for the Advancement of Science (AAAS)
- Herausgeber URL
- http://dx.doi.org/10.1126/scisignal.2000547
- Datum der Datenerfassung
- 2024
- Titel
- The Single Transmembrane Domains of Human Receptor Tyrosine Kinases Encode Self-Interactions
- Ausgabe der Zeitschrift
- 2
Data source: Crossref
- Other metadata sources:
-
- Abstract
- Transmembrane signaling by receptor tyrosine kinases typically involves a dynamic receptor monomer-dimer equilibrium in which ligand binding to soluble extracellular domains triggers receptor dimerization and subsequent signaling events. Although the role in signal transduction of the single transmembrane helices of individual receptors, which connect the extracellular with the intracellular protein domains, is not understood in detail, we show here that the single transmembrane domains of all 58 human receptor tyrosine kinases alone have an intrinsic propensity to form stable dimeric structures within a membrane. Thus, defined interactions of the transmembrane domains are most likely generally involved in signaling by all human receptor tyrosine kinases.
- Addresses
- Institut für Biochemie und Molekularbiologie, ZBMZ, Albert-Ludwigs-Universität, Freiburg, Germany.
- Autoren
- Carmen Finger
- Claudia Escher
- Dirk Schneider
- DOI
- 10.1126/scisignal.2000547
- eISSN
- 1937-9145
- Externe Identifier
- PubMed Identifier: 19797273
- Open access
- false
- ISSN
- 1945-0877
- Ausgabe der Veröffentlichung
- 89
- Zeitschrift
- Science signaling
- Schlüsselwörter
- Cell Membrane
- Humans
- Escherichia coli
- Receptor Protein-Tyrosine Kinases
- Recombinant Fusion Proteins
- Signal Transduction
- Binding Sites
- Amino Acid Sequence
- Protein Structure, Quaternary
- Protein Structure, Tertiary
- Dimerization
- Models, Biological
- Models, Molecular
- Molecular Sequence Data
- Protein Interaction Domains and Motifs
- In Vitro Techniques
- Sprache
- eng
- Medium
- Electronic
- Online publication date
- 2009
- Paginierung
- ra56
- Datum der Veröffentlichung
- 2009
- Status
- Published
- Datum der Datenerfassung
- 2009
- Titel
- The single transmembrane domains of human receptor tyrosine kinases encode self-interactions.
- Sub types
- Journal Article
- Ausgabe der Zeitschrift
- 2
Data source: Europe PubMed Central
- Abstract
- Transmembrane signaling by receptor tyrosine kinases typically involves a dynamic receptor monomer-dimer equilibrium in which ligand binding to soluble extracellular domains triggers receptor dimerization and subsequent signaling events. Although the role in signal transduction of the single transmembrane helices of individual receptors, which connect the extracellular with the intracellular protein domains, is not understood in detail, we show here that the single transmembrane domains of all 58 human receptor tyrosine kinases alone have an intrinsic propensity to form stable dimeric structures within a membrane. Thus, defined interactions of the transmembrane domains are most likely generally involved in signaling by all human receptor tyrosine kinases.
- Autoren
- Carmen Finger
- Claudia Escher
- Dirk Schneider
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/19797273
- DOI
- 10.1126/scisignal.2000547
- eISSN
- 1937-9145
- Ausgabe der Veröffentlichung
- 89
- Zeitschrift
- Sci Signal
- Schlüsselwörter
- Amino Acid Sequence
- Binding Sites
- Cell Membrane
- Dimerization
- Escherichia coli
- Humans
- In Vitro Techniques
- Models, Biological
- Models, Molecular
- Molecular Sequence Data
- Protein Interaction Domains and Motifs
- Protein Structure, Quaternary
- Protein Structure, Tertiary
- Receptor Protein-Tyrosine Kinases
- Recombinant Fusion Proteins
- Signal Transduction
- Sprache
- eng
- Country
- United States
- Paginierung
- ra56
- PII
- 2/89/ra56
- Datum der Veröffentlichung
- 2009
- Status
- Published online
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2009
- Titel
- The single transmembrane domains of human receptor tyrosine kinases encode self-interactions.
- Sub types
- Journal Article
- Ausgabe der Zeitschrift
- 2
Data source: PubMed
- Beziehungen:
- Property of