Membrane-bound LERK2 ligand can signal through three different Eph-related 
receptor tyrosine kinases

Brambilla, R.; Schnapp, A.; Casagranda, F.; Labrador, J. P.; Bergemann, A. D.; Flanagan, J. G.; Pasquale, E. B.; Klein, Rüdiger

doi:10.1002/j.1460-2075.1995.tb07314.x

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Membrane-bound LERK2 ligand can signal through three different Eph-related receptor tyrosine kinases

MPS-Authors

There are no MPG-Authors in the publication available

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Brambilla, R., Schnapp, A., Casagranda, F., Labrador, J. P., Bergemann, A. D., Flanagan, J. G., et al. (1995). Membrane-bound LERK2 ligand can signal through three different Eph-related receptor tyrosine kinases. The EMBO Journal, 14(13), 3116-3126. doi:10.1002/j.1460-2075.1995.tb07314.x.

Cite as: https://hdl.handle.net/21.11116/0000-0009-E379-F

Abstract

The Eph-related family of receptor tyrosine kinases consists of at least 13 members, several of which display distinctive expression patterns in the developing and adult nervous system. Recently, a small family of ligands, structurally related to the B61 protein, was identified. Binding of these ligands to Eph-related receptors did not, however, elicit measurable biological signals in cultured cells. In order to study functional interactions between B61-related ligands and Eph-related receptors, we constructed chimeric receptors, containing an Eph-related ectodomain and the cytoplasmic domain of the TrkB neurotrophin receptor. Expression and activation of such chimeric receptors in NIH 3T3 cells induced transformation in focus formation assays. Membrane-bound LERK2 ligand is shown to signal through three different Eph-related receptors, namely Cek5, Cek10 and Elk. LERK2, however, fails to interact functionally with the Cek9 receptor. Quantitative analysis including binding assays indicates that Cek10 is the preferred LERK2 receptor. Preliminary mutagenesis of the LERK2 protein suggests a negative regulatory role for its cytoplasmic domain in LERK2 signaling.