Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 389, Issue 1, Pages 10-16Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2009.04.002
Keywords
transmembrane helix; interaction; GxxxG; GG4; GALLEX
Categories
Funding
- Deutsche Forschungsgemeinschaft [SCHN 690/2-3, GRK 1478]
- Ministry of Science, Research and Arts of Baden-Wuttemberg
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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 heterooligomeric 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. (C) 2009 Elsevier Ltd. All rights reserved.
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