【摘 要】
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Cathepsin D (cathD) is traditionally regarded as a lysosomal protease that degrades substrates in acidic compartments.Here we report cathD plays an unconventional role as a cofilin phosphatase orchestrating actin remodeling.In neutral pH environments,the
【机 构】
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Department of Neurobiology and Department of Neurology of Second Affiliated Hospital,Zhejiang Univer
论文部分内容阅读
Cathepsin D (cathD) is traditionally regarded as a lysosomal protease that degrades substrates in acidic compartments.Here we report cathD plays an unconventional role as a cofilin phosphatase orchestrating actin remodeling.In neutral pH environments,the cathD precursor directly dephosphorylates and activates the actin-severing protein cofilin independent of its proteolytic activity,whereas mature cathD degrades coflin in acidic pH conditions.During development,cathD complements the canonical coflin phosphatase slingshot and regulates the morphogenesis of actin-based structures.Moreover,suppression of cathD phosphatase activity leads to defective actin organization and cytokinesis failure.Our findings identify cathD as a dual-function molecule,whose functional switch is regulated by environmental pH and its maturation state,and reveal a novel regulatory role of cathD in actin-based cellular processes.
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