HAI ‐2 stabilizes, inhibits, and regulates SEA‐cleavage‐dependent secretory transport of matriptase

We describe three mutations in the binding loop of the HAI‐2 Kunitz domain 1 (K42N, C47F, and R48L) that cause a delay in the SEA domain cleavage of matriptase, leading to accumulation of non‐SEA domain cleaved matriptase in the ER. Two of the HAI‐2 Kunitz domain 1 mutants investigated, C47F and R48L, also displayed a reduced ability to proteolytically silence matriptase, suggesting that HAI‐2 inhibits the proteolytic activity of matriptase in the secretory pathway.

Source: Traffic - March 28, 2017 Category: Research Authors: Annika W. Nonboe, Oliver Krigslund, Christoffer Soendergaard, Signe Skovbjerg, Stine Friis, Martin Nybo Andersen, Vincent Ellis, Makiko Kawaguchi, Hiroaki Kataoka, Thomas H. Bugge, Lotte K. Vogel Tags: ORIGINAL ARTICLE Source Type: research