Key result
Furin and site-1 protease cleave the prorenin receptor into soluble and transmembrane fragments.
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Generation of rats with a mutation in the (pro)renin receptor reveals its role in cellular functions, suggesting new therapeutic targets.
The (pro)renin receptor was initially identified as a receptor for renin and prorenin, and is now considered as a multifunctional protein involved in cellular homeostasis. In addition to mediating renin-angiotensin system activation, (pro)renin receptor contributes to vacuolar H+-ATPase function and Wnt signaling regulation. The full-length (pro)renin receptor undergoes post-translational cleavage by proteases including furin and site-1 protease (S1P) in the trans-Golgi network, generating two fragments: an N-terminal soluble form and a C-terminal transmembrane fragment.
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Hirose et al. (2026) studied this question. The (pro)renin receptor undergoes post-translational cleavage by furin and site-1 protease to generate an N-terminal soluble form and a C-terminal transmembrane fragment.
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