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Journal of Biochemistry Advance Access originally published online on August 1, 2006
Journal of Biochemistry 2006 140(3):445-452; doi:10.1093/jb/mvj170
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© 2006 The Japanese Biochemical Society.

ARTICLE

Multiple Processing of Ig-Hepta/GPR116, a G Protein–Coupled Receptor with Immunoglobulin (Ig)-Like Repeats, and Generation of EGF2-Like Fragment

Taku Fukuzawa and Shigehisa Hirose*

Department of Biological Sciences, Tokyo Institute of Technology, 4259-B19, Nagatsuta-cho, Midori-ku, Yokohama 226-8501

* To whom correspondence should be addressed. Tel: +81-45-924-5726, Fax: +81-45-924-5824, E-mail: shirose{at}bio.titech.ac.jp

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, {alpha}-fragment), (iii) Ig repeats (224–993, ß-chain), and (iv) TM7 (994–1349, {gamma}-chain). The proEGF2 region is converted to EGF2 (52–223) by the processing enzyme furin and remains attached to the ß- and {gamma}-chains. Expression of some mRNA species was affected by the presence of {alpha}-fragment. These results suggest that the furin-processed {alpha}-fragment is involved in cellular signaling.


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