Research article summary (published 20 Nov 2007):

The receptor protein tyrosine phosphatase PTP69D antagonizes Abl tyrosine kinase to guide axons in Drosophila.

Full Abstract

During Drosophila embryogenesis, both the cytoplasmic Abelson tyrosine kinase (Abl) and the membrane bound tyrosine phosphatase PTP69D are required for proper guidance of CNS and motor axons. We provide evidence that PTP69D modulates signaling by Abl and its antagonist, Ena. An Abl loss-of function mutation dominantly suppresses most Ptp69D mutant phenotypes including larval/pupal lethality and CNS and motor axon defects, while increased Abl and decreased Ena expression dramatically increase the expressivity of Ptp69D axonal defects. In contrast, Ptp69D mutations do not affect Abl mutant phenotypes. These results support the hypothesis that PTP69D antagonizes the Abl/Ena genetic pathway, perhaps as an upstream regulator. We also find that mutation of the gene encoding the cytoplasmic Src64B tyrosine kinase exacerbates Ptp69D phenotypes, suggesting that two different cytoplasmic tyrosine kinases, Abl and Src64B, modify PTP69D-mediated axon patterning in quite different ways.

Author information

Author/s: Song, Jeong K (JK); Giniger, Edward (E); Desai, Chand J (CJ);

Affiliation: Axon Guidance and Neural Connectivity Unit, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bldg 37 Room 1016, 37 Convent Drive, Bethesda, MD 20892, USA.

Grants: NSHD38141 (Agency:PHS HHS) ; R01 NS038141-01 (Agency:NINDS NIH HHS) ; R01 NS038141-02 (Agency:NINDS NIH HHS) ; R01 NS038141-03 (Agency:NINDS NIH HHS) ; R01 NS038141-04 (Agency:NINDS NIH HHS) ; R01 NS038141-05 (Agency:NINDS NIH HHS) ; Z01 NS003013-03 (Agency:NINDS NIH HHS)

Journal and publication information

Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, N.I.H., Intramural

Journal: Mechanisms of development (Mech Dev), published in Ireland. (Language: eng)

Reference: -2008 Mar-Apr; vol 125 (issue 3-4) : pp 247-56

Dates: Created 2008/02/12; Completed 2008/04/08; Revised 2009/03/04;

PMID: 18160268, status: MEDLINE (last retrieval date: 3/10/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Animals Axons - enzymology; physiology Body Patterning Central Nervous System - embryology; enzymology DNA-Binding Proteins - metabolism Drosophila - embryology; enzymology Drosophila Proteins - analysis; antagonists & inhibitors; genetics; metabolism Genes, Lethal

Humans Male Mutation Phenotype Protein-Tyrosine Kinases - analysis; antagonists & inhibitors; genetics; metabolism Proto-Oncogene Proteins - metabolism Receptor-Like Protein Tyrosine Phosphatases - genetics; metabolism Signal Transduction

Associated Chemicals: DNA-Binding Proteins (0) ; Drosophila Proteins (0) ; ENA/VASP proteins (0) ; Proto-Oncogene Proteins (0) ; Protein-Tyrosine Kinases (EC 2.7.1.112) ; Src64B protein, Drosophila (EC 2.7.1.112) ; abelson protein, Drosophila (EC 2.7.1.112) ; PTP69D protein, Drosophila (EC 3.1.3.48) ; Receptor-Like Protein Tyrosine Phosphatases (EC 3.1.3.48)

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