Multiple Processing of Ig-Hepta/GPR116, a G Protein–Coupled Receptor with Immunoglobulin (Ig)-Like Repeats, and Generation of EGF2-Like Fragment
Authors: Fukuzawa, Taku; Hirose, Shigehisa
Source: The Journal of Biochemistry, Volume 140, Number 3, September 2006 , pp. 445-452(8)
Publisher: Oxford University Press
Abstract:Ig-Hepta/GPR116 is a member of the LNB-TM7 subfamily of G protein–coupled receptors (GPCRs), also termed the adhesion GPCRs, whose members have EGF, cadherin, lectin, thrombospondin, or Ig repeats in their long N-terminus. In this study, we established that Ig-Hepta is processed at multiple sites yielding the following four fragments: (i) presequence (amino acid residues 1–24), (ii) proEGF2 (25–223, α-fragment), (iii) Ig repeats (224–993, -chain), and (iv) TM7 (994–1349, -chain). The proEGF2 region is converted to EGF2 (52–223) by the processing enzyme furin and remains attached to the - and -chains. Expression of some mRNA species was affected by the presence of α-fragment. These results suggest that the furin-processed α-fragment is involved in cellular signaling.
Document Type: Research Article
Publication date: September 2006