TY - JOUR
T1 - Neural expression of sorting nexin 25 and its regulation of tyrosine receptor kinase B trafficking
AU - Takemura, Shoko
AU - Isonishi, Ayami
AU - Tanaka, Tatsuhide
AU - Okuda, Hiroaki
AU - Tatsumi, Kouko
AU - Yamano, Mariko
AU - Wanaka, Akio
N1 - Publisher Copyright:
© 2020, Springer-Verlag GmbH Germany, part of Springer Nature.
PY - 2020/12
Y1 - 2020/12
N2 - Sorting nexin 25 (SNX25) belongs to the sorting nexin superfamily, whose members are responsible for membrane attachment to organelles of the endocytic system. Recent reports point to critical roles for SNX25 as a negative regulator of transforming growth factor β signaling, but the expression patterns of SNX25 in the central nervous system (CNS) remain almost uncharacterized. Here, we show widespread neuronal expression of SNX25 protein and Snx25 mRNA using immunohistochemistry and in situ hybridization. As an exception, SNX25 was present in the Bergmann glia of the cerebellum. SNX25 immunoreactivity was found in cholinergic and catecholaminergic neurons. Moreover, SNX25 colocalized with tropomyosin receptor kinase B (TrkB) in the neurons of the cortex and hippocampus. In vitro, SNX25 can interact with full-length TrkB, but not with its C-terminal-truncated isoform. Overexpression of SNX25 accelerated degradation of full-lengh TrkB, indicating that SNX25 promotes the trafficking of TrkB for lysosomal degradation. These findings suggest that SNX25 is a new actor in endocytic signaling, perhaps contributing to the regulation of BDNF–TrkB signaling in the CNS.
AB - Sorting nexin 25 (SNX25) belongs to the sorting nexin superfamily, whose members are responsible for membrane attachment to organelles of the endocytic system. Recent reports point to critical roles for SNX25 as a negative regulator of transforming growth factor β signaling, but the expression patterns of SNX25 in the central nervous system (CNS) remain almost uncharacterized. Here, we show widespread neuronal expression of SNX25 protein and Snx25 mRNA using immunohistochemistry and in situ hybridization. As an exception, SNX25 was present in the Bergmann glia of the cerebellum. SNX25 immunoreactivity was found in cholinergic and catecholaminergic neurons. Moreover, SNX25 colocalized with tropomyosin receptor kinase B (TrkB) in the neurons of the cortex and hippocampus. In vitro, SNX25 can interact with full-length TrkB, but not with its C-terminal-truncated isoform. Overexpression of SNX25 accelerated degradation of full-lengh TrkB, indicating that SNX25 promotes the trafficking of TrkB for lysosomal degradation. These findings suggest that SNX25 is a new actor in endocytic signaling, perhaps contributing to the regulation of BDNF–TrkB signaling in the CNS.
KW - BDNF
KW - Cortex
KW - Endosomal trafficking
KW - Hippocampus
KW - Lysosomal degradation
UR - https://www.scopus.com/pages/publications/85091254587
UR - https://www.scopus.com/pages/publications/85091254587#tab=citedBy
U2 - 10.1007/s00429-020-02144-0
DO - 10.1007/s00429-020-02144-0
M3 - Article
C2 - 32955616
AN - SCOPUS:85091254587
SN - 1863-2653
VL - 225
SP - 2615
EP - 2642
JO - Brain Structure and Function
JF - Brain Structure and Function
IS - 9
ER -