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PMID:21893139

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Citation

Overend, G, Cabrero, P, Guo, AX, Sebastian, S, Cundall, M, Armstrong, H, Mertens, I, Schoofs, L, Dow, JA and Davies, SA (2012) The receptor guanylate cyclase Gyc76C and a peptide ligand, NPLP1-VQQ, modulate the innate immune IMD pathway in response to salt stress. Peptides 34:209-18

Abstract

Receptorguanylate cyclases (rGCs) modulate diverse physiological processes including mammalian cardiovascular function and insect eclosion. The Drosophila genome encodes several receptor and receptor-like GCs, but no ligand for any Drosophila rGC has yet been identified. By screening peptide libraries in Drosophila S2 cells, the Drosophila peptide NPLP1-VQQ (NLGALKSSPVHGVQQ) was shown to be a ligand for the rGC, Gyc76C (CG42636, previously CG8742, l(3)76BDl, DrGC-1). In the adult fly, expression of Gyc76C is highest in immune and stress-sensing epithelial tissues, including Malpighian tubules and midgut; and NPLP1-VQQ stimulates fluid transport and increases cGMP content in tubules. cGMP signaling is known to modulate the activity of the IMD innate immune pathway in tubules via activation and nuclear translocation of the NF-kB orthologue, Relish, resulting in increased anti-microbial peptide (AMP) gene expression; and so NPLP1-VQQ might act in immune/stress responses. Indeed, NPLP1-VQQ induces nuclear translocation of Relish in intact tubules and increases expression of the anti-microbial peptide gene, diptericin. Targeted Gyc76C RNAi to tubule principal cells inhibited both NPLP1-VQQ-induced Relish translocation and diptericin expression. Relish translocation and increased AMP gene expression also occurs in tubules in response to dietary salt stress. Gyc76C also modulates organismal survival to salt stress - ablation of Gyc76C expression in only tubule principal cells prevents Relish translocation, reduces diptericin expression, and reduces organismal survival in response to salt stress. Thus, the principal-cell localized NPLP1-VQQ/Gyc76C cGMP pathway acts to signal environmental (salt) stress to the whole organism.

Links

PubMed Online version:10.1016/j.peptides.2011.08.019

Keywords

Amino Acid Sequence; Animals; Drosophila; Drosophila Proteins/genetics; Drosophila Proteins/metabolism; Guanylate Cyclase/genetics; Guanylate Cyclase/metabolism; Immunity, Innate/drug effects; Immunity, Innate/genetics; Molecular Sequence Data; Neuropeptides/metabolism; Neuropeptides/pharmacology; Sodium Chloride/pharmacology

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

DROME:GC76C

located_in

GO:0005887: integral component of plasma membrane

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:GC76C

involved_in

GO:0009651: response to salt stress

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

DROME:GC76C

involved_in

GO:0007168: receptor guanylyl cyclase signaling pathway

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

DROME:GC76C

enables

GO:0001653: peptide receptor activity

ECO:0000353: physical interaction evidence used in manual assertion

FB:FBgn0035092

F

Seeded From UniProt

complete

DROME:GC76C

enables

GO:0004383: guanylate cyclase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

DROME:NPLP1

enables

GO:0005184: neuropeptide hormone activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

DROME:NPLP1

located_in

GO:0005615: extracellular space

ECO:0000305: curator inference used in manual assertion

GO:0048018

C

Seeded From UniProt

complete

DROME:NPLP1

involved_in

GO:0007168: receptor guanylyl cyclase signaling pathway

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

DROME:NPLP1

enables

GO:0048018: receptor ligand activity

ECO:0000353: physical interaction evidence used in manual assertion

FB:FBgn0266136

F

Seeded From UniProt

complete


See also

References

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