Regulation of multimers via truncated isoforms: a novel mechanism to control nitric-oxide signaling

Stasiv, Y., Kuzin, B., Regulski, M., Tully, T., Enikolopov, G. (August 2004) Regulation of multimers via truncated isoforms: a novel mechanism to control nitric-oxide signaling. Genes Dev, 18 (15). pp. 1812-23. ISSN 0890-9369 (Print)

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URL: https://www.ncbi.nlm.nih.gov/pubmed/15256486
DOI: 10.1101/gad.298004

Abstract

Nitric oxide (NO) is an essential regulator of Drosophila development and physiology. We describe a novel mode of regulation of NO synthase (NOS) function that uses endogenously produced truncated protein isoforms of Drosophila NOS (DNOS). These isoforms inhibit NOS enzymatic activity in vitro and in vivo, reflecting their ability to form complexes with the full-length DNOS protein (DNOS1). Truncated isoforms suppress the antiproliferative action of DNOS1 in the eye imaginal disc by impacting the retinoblastoma-dependent pathway, yielding hyperproliferative phenotypes in pupae and adult flies. Our results indicate that endogenous products of the dNOS locus act as dominant negative regulators of NOS activity during Drosophila development.

Item Type: Paper
Uncontrolled Keywords: Alternative Splicing Animals Animals, Genetically Modified Bromodeoxyuridine/diagnostic use Cell Division Cells, Cultured Drosophila/ enzymology/genetics/growth & development Enzyme Inhibitors/pharmacology Eye/drug effects/ growth & development Free Radical Scavengers/ pharmacology Gene Expression Regulation, Developmental Genes, Dominant Nitric Oxide/ pharmacology Nitric Oxide Synthase/antagonists & inhibitors/genetics/ metabolism Phenotype Protein Isoforms Pupa/growth & development Retinoblastoma Protein/metabolism S Phase Signal Transduction/drug effects
CSHL Authors:
Communities: CSHL labs > Enikopolov lab
Depositing User: CSHL Librarian
Date: 1 August 2004
Date Deposited: 17 Jan 2012 19:58
Last Modified: 01 Mar 2017 17:04
PMCID: PMC517402
Related URLs:
URI: http://repository.cshl.edu/id/eprint/22488

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