Two GxxxG-Like Motifs Facilitate Promiscuous Interactions of the Human ErbB Transmembrane Domains

Publication type:
Journal article
Metadata:
Autoren
  • Claudia Escher
  • Florian Cymer
  • Dirk Schneider
DOI
10.1016/j.jmb.2009.04.002
ISSN
0022-2836
Ausgabe der Veröffentlichung
1
Zeitschrift
Journal of Molecular Biology
Sprache
en
Paginierung
10 - 16
Datum der Veröffentlichung
2009
Status
Published
Herausgeber
Elsevier BV
Herausgeber URL
http://dx.doi.org/10.1016/j.jmb.2009.04.002
Datum der Datenerfassung
2018
Titel
Two GxxxG-Like Motifs Facilitate Promiscuous Interactions of the Human ErbB Transmembrane Domains
Ausgabe der Zeitschrift
389

Data source: Crossref

Other metadata sources:
Abstract
Members of the ErbB/HER family of epidermal growth factor receptor tyrosine kinases cross a membrane with a single transmembrane (TM) helix. ErbB receptors form diverse homo- and heterodimers, which substantially increases the signaling potential of ErbB receptors. The involvement of the ErbB TM domains in homo- and heterodimerization is largely enigmatic. In this study, we experimentally analyzed the potential role of two conserved GxxxG-like motifs for mediating and/or stabilizing homo- and hetero-oligomeric interactions of the human ErbB TM domains. Both motifs appear to be critical for homo- and hetero-oligomeric TM helix interactions. Consequently, multiple TM structures are possible for the various ErbB homo- and heterodimers, which might be critical for the formation and TM signaling of specific ErbB pairs in vivo.
Addresses
  • Institut für Biochemie und Molekularbiologie, ZBMZ, Albert-Ludwigs-Universität, Freiburg, Germany.
Autoren
  • Claudia Escher
  • Florian Cymer
  • Dirk Schneider
DOI
10.1016/j.jmb.2009.04.002
eISSN
1089-8638
Externe Identifier
  • PubMed Identifier: 19361517
Open access
false
ISSN
0022-2836
Ausgabe der Veröffentlichung
1
Zeitschrift
Journal of molecular biology
Schlüsselwörter
  • Humans
  • Receptor Protein-Tyrosine Kinases
  • Amino Acid Sequence
  • Amino Acid Motifs
  • Protein Structure, Tertiary
  • Protein Binding
  • Structure-Activity Relationship
  • Mutation
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Multimerization
Sprache
eng
Medium
Print-Electronic
Online publication date
2009
Paginierung
10 - 16
Datum der Veröffentlichung
2009
Status
Published
Datum der Datenerfassung
2009
Titel
Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains.
Sub types
  • Research Support, Non-U.S. Gov't
  • Journal Article
Ausgabe der Zeitschrift
389

Data source: Europe PubMed Central

Abstract
Members of the ErbB/HER family of epidermal growth factor receptor tyrosine kinases cross a membrane with a single transmembrane (TM) helix. ErbB receptors form diverse homo- and heterodimers, which substantially increases the signaling potential of ErbB receptors. The involvement of the ErbB TM domains in homo- and heterodimerization is largely enigmatic. In this study, we experimentally analyzed the potential role of two conserved GxxxG-like motifs for mediating and/or stabilizing homo- and hetero-oligomeric interactions of the human ErbB TM domains. Both motifs appear to be critical for homo- and hetero-oligomeric TM helix interactions. Consequently, multiple TM structures are possible for the various ErbB homo- and heterodimers, which might be critical for the formation and TM signaling of specific ErbB pairs in vivo.
Date of acceptance
2009
Autoren
  • Claudia Escher
  • Florian Cymer
  • Dirk Schneider
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/19361517
DOI
10.1016/j.jmb.2009.04.002
eISSN
1089-8638
Ausgabe der Veröffentlichung
1
Zeitschrift
J Mol Biol
Schlüsselwörter
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Protein Binding
  • Protein Multimerization
  • Protein Structure, Tertiary
  • Receptor Protein-Tyrosine Kinases
  • Structure-Activity Relationship
Sprache
eng
Country
Netherlands
Paginierung
10 - 16
PII
S0022-2836(09)00402-1
Datum der Veröffentlichung
2009
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2009
Titel
Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
389

Data source: PubMed

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