Lysosomal Hydrolase Cathepsin D Non-proteolytically Modulates Dendritic Morphology in Drosophila.
10.1007/s12264-020-00479-6
- Author:
Ting ZHANG
1
;
Daxiao CHENG
1
;
Cunjin WU
1
;
Xingyue WANG
1
;
Qiang KE
2
;
Huifang LOU
1
;
Liya ZHU
1
;
Xiao-Dong WANG
1
;
Shumin DUAN
3
;
Yi-Jun LIU
4
Author Information
1. Department of Neurobiology, Key Laboratory of Medical Neurobiology of the Ministry of Health of China, Zhejiang Province Key Laboratory of Neurobiology, Zhejiang University School of Medicine, Hangzhou, 310058, China.
2. Department of Diagnostics, Hangzhou Normal University Medical School, Hangzhou, 311121, China.
3. Department of Neurobiology, Key Laboratory of Medical Neurobiology of the Ministry of Health of China, Zhejiang Province Key Laboratory of Neurobiology, Zhejiang University School of Medicine, Hangzhou, 310058, China. duanshumin@zju.edu.cn.
4. Department of Neurobiology, Key Laboratory of Medical Neurobiology of the Ministry of Health of China, Zhejiang Province Key Laboratory of Neurobiology, Zhejiang University School of Medicine, Hangzhou, 310058, China. yjliu@zju.edu.cn.
- Publication Type:Journal Article
- Keywords:
Actin;
Cathepsin D;
Dendritic arborization;
Drosophila;
Mushroom body;
Sensory neuron
- From:
Neuroscience Bulletin
2020;36(10):1147-1157
- CountryChina
- Language:English
-
Abstract:
The main lysosomal protease cathepsin D (cathD) is essential for maintaining tissue homeostasis via its degradative function, and its loss leads to ceroid accumulation in the mammalian nervous system, which results in progressive neurodegeneration. Increasing evidence implies non-proteolytic roles of cathD in regulating various biological processes such as apoptosis, cell proliferation, and migration. Along these lines, we here showed that cathD is required for modulating dendritic architecture in the nervous system independent of its traditional degradative function. Upon cathD depletion, class I and class III arborization (da) neurons in Drosophila larvae exhibited aberrant dendritic morphology, including over-branching, aberrant turning, and elongation defects. Re-introduction of wild-type cathD or its proteolytically-inactive mutant dramatically abolished these morphological defects. Moreover, cathD knockdown also led to dendritic defects in the adult mushroom bodies, suggesting that cathD-mediated processes are required in both the peripheral and central nervous systems. Taken together, our results demonstrate a critical role of cathD in shaping dendritic architecture independent of its proteolytic function.
