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Regulation of lysosomal positioning via TMEM55B phosphorylation
Abstract
Lysosomes are dynamic organelles that are transported along microtubules bidirectionally via kinesin and dynein motor proteins. Lysosomal positioning, which is determined by the balance of the bidirectional lysosomal movement, changes under various conditions and affects lysosomal functions such as autophagy and antigen presentation. A recent study by Takemasu et al. (Phosphorylation of TMEM55B by Erk/MAPK regulates lysosomal positioning. J. Biochem. 2019; 166:175–185) has shown that phosphorylation of the transmembrane protein TMEM55B is involved in the retrograde lysosomal trafficking towards the perinuclear region. They found that TMEM55B is phosphorylated upon stimulation with various ligands and that Erk/MAPK mediates the TMEM55B phosphorylation. They have also revealed that a phosphorylation mimic mutant of TMEM55B enhances perinuclear lysosomal clustering compared to the wild-type TMEM55B. These findings suggest that TMEM55B phosphorylation by Erk/MAPK is responsible for regulating lysosomal positioning in response to external stimuli.
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TMEM55B (PIP4P1) is a key player in the retrograde trafficking of lysosomes in multiple cell types.
“Transmembrane protein 55B (TMEM55B), also known as phosphatidylinositol-4,5bisphosphate 4-phosphatase 1 (PIP4P1), is a key player in the retrograde trafficking of lysosomes in multiple cell types (Araki & Kontani, 2021;Rudnik et al., 2022;Takemasu et al., 2019;Willett et al., 2017).”
From Hippocampal TMEM55B overexpression in the 5XFAD mouse model of Alzheimer's disease (2024) · cites this paper as Araki & Kontani, 2021
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Hippocampal TMEM55B overexpression in the 5XFAD mouse model of Alzheimer's disease
Odfalk, K. F., Wickline, J. L., Smith, S., Dobrowolski, R., & Hopp, S. C. (2024) · Hippocampus · doi:10.1002/hipo.23586 · Cited by 2
Metadata
- Authors
- Araki, M., & Kontani, K.
- Affiliations
- Department of Biochemistry, Meiji Pharmaceutical University, 2-522-1 Noshio, Kiyose, Tokyo 204-8588, Japan
- ORCID
- Kontani, Kenji
- Venue
- The Journal of Biochemistry
- Publisher
- Oxford University Press (OUP)
- Published
- 2021-02-04
- Volume
- 169
- Issue
- 5
- Pages
- 507-509
- ISSN
- 0021-924X
- 1756-2651
- Cited by
- 7
- References
- 3
- Language
- en
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