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Open AccessJournal ArticleDOI

Drosophila RET contains an active tyrosine kinase and elicits neurotrophic activities in mammalian cells

Chiara Abrescia, +3 more
- 04 Jul 2005 - 
- Vol. 579, Iss: 17, pp 3789-3796
TLDR
Initial biochemical and functional characterization of the dRET protein in cell culture systems indicate significant conservation between the biological effects elicited by the human and Drosophila RET kinases, and suggest functions for dRET in neuronal differentiation in the fly.
About
This article is published in FEBS Letters.The article was published on 2005-07-04 and is currently open access. It has received 32 citations till now. The article focuses on the topics: Glial cell line-derived neurotrophic factor & Tyrosine phosphorylation.

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Citations
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Journal ArticleDOI

Structure and Physiology of the RET Receptor Tyrosine Kinase

TL;DR: The discovery of ret opened a field of study that has had a profound impact in cancer research, developmental biology, and neuroscience, and that continues to yield surprises and important insights to this day.

Coordinated Activation of Autophosphorylation Sites in the RET

TL;DR: The catalytic and signaling activities of RET, a tyrosine kinase receptor for glial cell line-derived neurotrophic factor (GDNF), are controlled by the autophosphorylation of several tyrosines in the RET cytoplasmic domain this article.
Journal ArticleDOI

Evolution of the GDNF family ligands and receptors.

TL;DR: The presence of RET- and GFR-like genes in insects suggests that a ProtoGFR and a ProtoRET arose early in the evolution of bilaterian animals, but when the ProtoGFL diverged from existing transforming growth factor (TGFβ)-like proteins remains unclear.
Journal ArticleDOI

Receptor Tyrosine Kinases in Drosophila Development

TL;DR: A comprehensive review of what is known regarding each receptor tyrosine kinase during Drosophila development highlights the importance of knowing the structure and function of these enzymes in the context of cell survival and proliferation.
References
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Journal ArticleDOI

Characterization of a multicomponent receptor for GDNF

TL;DR: It is demonstrated that physiological responses to GDNF require the presence of a novel glycosyl-phosphatidylinositol (GPI)-linked protein (designated GDNFR-α) that is expressed on GDNF-responsive cells and binds GDNF with a high affinity, which supports the hypothesis that GDNF uses a multi-subunit receptor system in which GDN FR-α and Ret function as the ligand-binding and signalling components.
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Neurotrophins: key regulators of cell fate and cell shape in the vertebrate nervous system

TL;DR: The most primitive neurotrophin genes have been isolated from jawless fishes, a river lamprey and the Atlantic hagfish, and they encode pre-pro-neurotrophins, which may serve the purpose of limiting their range of action.
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Functional receptor for GDNF encoded by the c-ret proto-oncogene.

TL;DR: It is shown that GDNF binds to, and induces tyrosine phosphorylation of, the product of the c-ret proto-oncogene, an orphan receptor tyrosin kinase, in a GDNF responsive motor-neuron cell line, which encodes a functional receptor for GDNF that may mediate its neurotrophic effects on motor and dopaminergic neurons.
Journal ArticleDOI

Phylogenetic analysis of the cadherin superfamily allows identification of six major subfamilies besides several solitary members.

TL;DR: In this paper, a phylogenetic analysis of the cadherin superfamily is presented, which can be distinguished on the basis of protein domain composition, genomic structure, and phylogenetic analyses of the protein sequences.
Journal ArticleDOI

The neural cell adhesion molecule NCAM is an alternative signaling receptor for GDNF family ligands.

TL;DR: The results uncover an unexpected intersection between short- and long-range mechanisms of intercellular communication and reveal a pathway for GDNF signaling that does not require the RET receptor.
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