Requirement of Drosophila NF1 for Activation of Adenylyl Cyclase by PACAP38-Like Neuropeptides

Author:

Guo Hui-Fu12,The Inge12,Hannan Frances12,Bernards André12,Zhong Yi12

Affiliation:

1. H.-F. Guo, F. Hannan, Y. Zhong, Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA.

2. I. The and A. Bernards, Massachusetts General Hospital Cancer Center, Building 149, 13th Street, Charlestown, MA 02129, USA.

Abstract

The human neurofibromatosis type 1 (NF1) tumor suppressor protein functions as a Ras-specific guanosine triphosphatase–activating protein, but the identity of Ras- mediated pathways modulated by NF1 remains unknown. A study of Drosophila NF1 mutants revealed that NF1 is essential for the cellular response to the neuropeptide PACAP38 (pituitary adenylyl cyclase–activating polypeptide) at the neuromuscular junction. The peptide induced a 100-fold enhancement of potassium currents by activating the Ras-Raf and adenylyl cyclase–adenosine 3’,5’-monophosphate (cAMP) pathways. This response was eliminated in NF1 mutants. NF1 appears to regulate the rutabaga -encoded adenylyl cyclase rather than the Ras-Raf pathway. Moreover, the NF1 defect was rescued by the exposure of cells to pharmacological treatment that increased concentrations of cAMP.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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