In silico discovery of the first putative receptors from the American lobster, Homarus americanus


Meeting Abstract

P3-136  Wednesday, Jan. 6 15:30  In silico discovery of the first putative receptors from the American lobster, Homarus americanus LAMEYER, T.J.*; PASCUAL, M.G.; STANHOPE, M.E.; CHI, M.; SHEA, D.N.; MARDER, E.; SCHULTZ, D.J.; DICKINSON, P.S.; CHRISTIE, A.E.; Bowdoin College, Brunswick, ME 04011; University of Hawaii at Manoa, Honolulu, HI 96822; Bowdoin College, Brunswick, ME 04011; University of Hawaii at Manoa, Honolulu, HI 96822; Bowdoin College, Brunswick, ME 04011; University of Missouri, Columbia, MO 65211; Brandeis University, Waltham, MA 02454; Bowdoin College, Brunswick, ME 04011; University of Hawaii at Manoa, Honolulu, HI 96822 tlameyer@bowdoin.edu

The molecular components of peptidergic signaling systems in nervous systems include both neuropeptides and peptide receptors. In the lobster, Homarus americanus, numerous neuropeptides have been identified and characterized. In contrast, nothing is known about the identity of neuropeptide receptors in this species. Here, known peptide receptors, primarily ones from the fruit fly, Drosophila melanogaster, were used to mine a H. americanus neural transcriptome for sequences encoding homologous proteins. Via this strategy, over 40 putative receptor-encoding transcripts were identified. The proteins deduced from these receptors include putative adipokinetic hormone-corazonin-like peptide, allatostatin A, allatostatin C (AST-C), bursicon, CCHamide, corazonin, crustacean cardioactive peptide, diuretic hormone 31, diuretic hormone 44, ecdysis-triggering hormone, FLRFamide, insulin-like peptide, leucokinin, myosuppressin, neuropeptide F, pigment dispersing hormone, proctolin, pyrokinin, red pigment concentrating hormone, SIFamide, sulfakinin and tachykinin-related peptide receptors. For many peptide groups, multiple receptor subtypes appear to exist in the lobster. For example, three distinct proteins showing homology to known AST-C receptors were discovered. Structural analysis of the full-length proteins showed the majority of them to possess complements of structural motifs consistent with their proposed function as peptide receptors, e.g. seven membrane spanning regions, and, in some cases, hormone-binding domains.

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