Receptor tyrosine kinase transmembrane domains

Function, dimer structure and dimerization energetics

Research output: Contribution to journalArticle

Abstract

The transmembrane (TM) domains of receptor tyrosine kinases (RTKs) play an active role in signaling. They contribute to the stability of full-length receptor dimers and to maintaining a signaling-competent dimeric receptor conformation. In an exciting new development, two structures of RTK TM domains have been solved, a break-through achievement in the field. here we review these structures, and we discuss recent studies of RTK TM domain dimerization energetics, possible synergies between domains, and the effects of pathogenic RTK TM mutations on structure and dimerization.

Original languageEnglish (US)
Pages (from-to)249-254
Number of pages6
JournalCell Adhesion and Migration
Volume4
Issue number2
DOIs
StatePublished - 2010

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Receptor Protein-Tyrosine Kinases
Dimerization
Mutation

Keywords

  • Dimer structure
  • Dimerization thermodynamics
  • Pathogenic mutations
  • Receptor tyrosine kinases
  • Transmembrane domain

ASJC Scopus subject areas

  • Cell Biology
  • Cellular and Molecular Neuroscience
  • Medicine(all)

Cite this

Receptor tyrosine kinase transmembrane domains : Function, dimer structure and dimerization energetics. / Li, Edwin; Hristova, Kalina A.

In: Cell Adhesion and Migration, Vol. 4, No. 2, 2010, p. 249-254.

Research output: Contribution to journalArticle

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