ArticleThe EMBO journal1995
Membrane-bound LERK2 ligand can signal through three different Eph-related receptor tyrosine kinases.
Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.
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Who cites it
26 citing papers in PubMed, 1 synthesis or guideline pooled it.
- The Value of EphB2 Receptor and Cognate Ephrin Ligands in Prognostic and Predictive Assessments of Human Breast Cancer.International journal of molecular sciences · 2021Pooled it
- Article
- EphrinB2-EphB4-RASA1 Signaling in Human Cerebrovascular Development and Disease.Trends in molecular medicine · 2019Review
- EphB3 Stimulates Cell Migration and Metastasis in a Kinase-dependent Manner through Vav2-Rho GTPase Axis in Papillary Thyroid Cancer.The Journal of biological chemistry · 2017Article
- The coexpression of EphB4 and EphrinB2 is associated with poor prognosis in HER2-positive breast cancer.OncoTargets and therapy · 2017Article
- EphA5 and EphA6: regulation of neuronal and spine morphology.Cell & bioscience · 2016Article
- Regulation of tumor initiation and metastatic progression by Eph receptor tyrosine kinases.Advances in cancer research · 2012Review
- Distribution of EphA5 receptor protein in the developing and adult mouse nervous system.The Journal of comparative neurology · 2009Article
- Treatment with ephrin B2 positively impacts the abnormal metabolism of human osteoarthritic chondrocytes.Arthritis research & therapy · 2009Article
- Coexpression of EphB4 and ephrinB2 in tumour advancement of ovarian cancers.British journal of cancer · 2008Article
- EphB receptors regulate stem/progenitor cell proliferation, migration, and polarity during hippocampal neurogenesis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
- Article
- ERK1 and ERK2 mitogen-activated protein kinases affect Ras-dependent cell signaling differentially.Journal of biology · 2006Article
- LMW-PTP is a positive regulator of tumor onset and growth.Oncogene · 2004Article
- A new ephrin-A1 isoform (ephrin-A1b) with altered receptor binding properties abrogates the cleavage of ephrin-A1a.The Biochemical journal · 2004Article
- Tyr-298 in ephrinB1 is critical for an interaction with the Grb4 adaptor protein.The Biochemical journal · 2004Article
- Downregulation of the Ras-mitogen-activated protein kinase pathway by the EphB2 receptor tyrosine kinase is required for ephrin-induced neurite retraction.Molecular and cellular biology · 2001Article
- Growth factor signaling pathways in vascular development.Oncogene · 1999Review
- Article
- Roles of ephrinB ligands and EphB receptors in cardiovascular development: demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis.Genes & development · 1999Article
Corrections and comments
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Authors and funding
8 authors.
Funding
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.
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