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Journal of Biochemistry Advance Access published online on August 1, 2006
Journal of Biochemistry, doi:10.1093/jb/mvj170
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© 2006 The Japanese Biochemical Society.
Received July 9, 2006
Accepted July 27, 2006

Regular Paper

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

Taku Fukuzawa 1 and Shigehisa Hirose 1 *

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

* To whom correspondence should be addressed.
Shigehisa Hirose, E-mail: shirose{at}bio.titech.ac.jp


  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, {alpha}-fragment), (iii) Ig repeats (224-993, {beta}-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 {beta}- 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.

Keywords: furin; G protein-coupled receptor; LNB-TM7; proteolytic processing; SEA module.
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