Abstract:
:Retention of intron 8 in alternative HER-2 mRNA generates an inhibitory secreted ligand, Herstatin, with a novel receptor-binding domain (RBD) encoded by the intron. This study examines binding interactions with several receptors and investigates sequence variations in intron 8. The RBD, expressed as a peptide, binds at nM concentrations to HER-2, the EGFR, DeltaEGFR, HER-4 and to the IGF-1 receptor, but not to HER-3 nor to the FGF-3 receptor, whereas a rare mutation in the RBD (Arg to Ile) eliminates receptor binding. The full-length Herstatin binds with 3-4-fold higher affinity than its RBD, but with approximately 10-fold lower affinity to the IGF-IR. Sequence conservation in rhesus monkey but not in rat suggests that intron 8 recently diverged as a receptor-binding module critical for the function of Herstatin.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Shamieh LS,Evans AJ,Denton MC,Clinton GMdoi
10.1016/j.febslet.2004.05.027keywords:
subject
Has Abstractpub_date
2004-06-18 00:00:00pages
163-6issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579304006489journal_volume
568pub_type
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