Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

Sci. Signal., 22 September 2009
Vol. 2, Issue 89, p. ra56
[DOI: 10.1126/scisignal.2000547]

RESEARCH ARTICLES

The Single Transmembrane Domains of Human Receptor Tyrosine Kinases Encode Self-Interactions

Carmen Finger1,2*, Claudia Escher1*, and Dirk Schneider1{dagger}

1 Institut für Biochemie und Molekularbiologie, ZBMZ, Albert-Ludwigs-Universität, Stefan-Meier-Strasse 17, 79104 Freiburg, Germany.
2 Fakultät für Biologie, Albert-Ludwigs-Universität, Stefan-Meier-Strasse 17, 79104 Freiburg, Germany.

* These authors contributed equally to this work.

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.

{dagger} To whom correspondence should be addressed. E-mail: Dirk.Schneider{at}biochemie.uni-freiburg.de

Citation: C. Finger, C. Escher, D. Schneider, The Single Transmembrane Domains of Human Receptor Tyrosine Kinases Encode Self-Interactions. Sci. Signal. 2, ra56 (2009).

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Glycosylation at Asn211 Regulates the Activation State of the Discoidin Domain Receptor 1 (DDR1).
H.-L. Fu, R. R. Valiathan, L. Payne, M. Kumarasiri, K. V. Mahasenan, S. Mobashery, P. Huang, and R. Fridman (2014)
J. Biol. Chem. 289, 9275-9287
   Abstract »    Full Text »    PDF »
Hepatitis C Virus RNA Replication and Virus Particle Assembly Require Specific Dimerization of the NS4A Protein Transmembrane Domain.
A. Kohlway, N. Pirakitikulr, F. N. Barrera, O. Potapova, D. M. Engelman, A. M. Pyle, and B. D. Lindenbach (2014)
J. Virol. 88, 628-642
   Abstract »    Full Text »    PDF »
Homodimerization of the Wnt Receptor DERAILED Recruits the Src Family Kinase SRC64B.
I. M. Petrova, L. L. Lahaye, T. Martianez, A. W. M. de Jong, M. J. Malessy, J. Verhaagen, J. N. Noordermeer, and L. G. Fradkin (2013)
Mol. Cell. Biol. 33, 4116-4127
   Abstract »    Full Text »    PDF »
Protein engineering methods applied to membrane protein targets.
M. W. Lluis, J. I. Godfroy III, and H. Yin (2013)
Protein Eng. Des. Sel. 26, 91-100
   Abstract »    Full Text »    PDF »
A Transmembrane Domain and GxxxG Motifs within L2 Are Essential for Papillomavirus Infection.
M. P. Bronnimann, J. A. Chapman, C. K. Park, and S. K. Campos (2013)
J. Virol. 87, 464-473
   Abstract »    Full Text »    PDF »
Thermostability of Two Cyanobacterial GrpE Thermosensors.
S. Barthel, E. Rupprecht, and D. Schneider (2011)
Plant Cell Physiol. 52, 1776-1785
   Abstract »    Full Text »    PDF »
Structural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex.
K. Verstraete, G. Vandriessche, M. Januar, J. Elegheert, A. V. Shkumatov, A. Desfosses, K. Van Craenenbroeck, D. I. Svergun, I. Gutsche, B. Vergauwen, et al. (2011)
Blood 118, 60-68
   Abstract »    Full Text »    PDF »
The Extracellular Domain of Fibroblast Growth Factor Receptor 3 Inhibits Ligand-Independent Dimerization.
L. Chen, J. Placone, L. Novicky, and K. Hristova (2010)
Science Signaling 3, ra86
   Abstract »    Full Text »    PDF »
Receptor Tyrosine Kinase Transmembrane Domain Interactions: Potential Target for "Interceptor" Therapy.
A. K. Najumudeen (2010)
Science Signaling 3, jc6
   Abstract »    Full Text »    PDF »

To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882