Drosophila molting neurohormone bursicon is a heterodimer and the natural agonist of the orphan receptor DLGR2.

TY - JOUR

T1 - Drosophila molting neurohormone bursicon is a heterodimer and the natural agonist of the orphan receptor DLGR2.

AU - Mendive, Fernando M

AU - Van Loy, Tom

AU - Claeysen, Sylvie

AU - Poels, Jeroen

AU - Williamson, Michael

AU - Hauser, Frank

AU - Grimmelikhuijzen, Cornelis J P

AU - Vassart, Gilbert

AU - Vanden Broeck, Jozef

N1 - Keywords: Amino Acid Sequence; Animals; Chromatography, Gel; Culture Media, Conditioned; Dimerization; Drosophila; Invertebrate Hormones; Molecular Sequence Data; Open Reading Frames; RNA, Messenger; Receptors, G-Protein-Coupled; Sequence Homology, Amino Acid

PY - 2005

Y1 - 2005

N2 - Bursicon is a neurohumoral agent responsible for tanning and hardening of the cuticle and expansion of the wings during the final phase of insect metamorphosis. Although the hormonal activity was described more than 40 years ago, the molecular nature of bursicon has remained elusive. We identify here Drosophila bioactive bursicon as a heterodimer made of two cystine knot polypeptides. This conclusion was reached in part from the unexpected observation that in the genome of the honey bee, the orthologs of the two Drosophila proteins are predicted to be fused in a single open reading frame. The heterodimeric Drosophila protein displays bursicon bioactivity in freshly enclosed neck-ligated flies and is the natural agonist of the orphan G protein-coupled receptor DLGR2.

AB - Bursicon is a neurohumoral agent responsible for tanning and hardening of the cuticle and expansion of the wings during the final phase of insect metamorphosis. Although the hormonal activity was described more than 40 years ago, the molecular nature of bursicon has remained elusive. We identify here Drosophila bioactive bursicon as a heterodimer made of two cystine knot polypeptides. This conclusion was reached in part from the unexpected observation that in the genome of the honey bee, the orthologs of the two Drosophila proteins are predicted to be fused in a single open reading frame. The heterodimeric Drosophila protein displays bursicon bioactivity in freshly enclosed neck-ligated flies and is the natural agonist of the orphan G protein-coupled receptor DLGR2.

U2 - 10.1016/j.febslet.2005.03.006

DO - 10.1016/j.febslet.2005.03.006

M3 - Journal article

C2 - 15811337

SN - 0014-5793

VL - 579

SP - 2171

EP - 2176

JO - FEBS Letters

JF - FEBS Letters

IS - 10

ER -