AI Article Synopsis
- Lysosomes are organelles that move along microtubules with the help of kinesin and dynein motor proteins, influencing their position and functions like autophagy.
- A study by Takemasu et al. found that the phosphorylation of TMEM55B, a transmembrane protein, plays a critical role in the movement of lysosomes back to the perinuclear region.
- The research indicates that when TMEM55B is phosphorylated by Erk/MAPK, it enhances lysosomal clustering near the nucleus, revealing how external signals can affect lysosomal positioning.
Article 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.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1093/jb/mvab013 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
RpH-ILV: Probe for lysosomal pH and acute LLOMe-induced membrane permeabilization in cell lines and .
Sci Adv
January 2025
Department of Biochemistry Cell and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, UK.
Lysosomal pH dysregulation is a critical element of the pathophysiology of neurodegenerative diseases, cancers, and lysosomal storage disorders (LSDs). To study the role of lysosomes in pathophysiology, probes to analyze lysosomal size, positioning, and pH are indispensable tools. Here, we developed and characterized a ratiometric genetically encoded lysosomal pH probe, RpH-ILV, targeted to a subpopulation of lysosomal intraluminal vesicles.
View Article and Find Full Text PDFSelf-assembled eumelanin nanoparticles enhance IFN-I activation and cilia-driven intercellular communication to defend against Tulane virus, a human norovirus surrogate.
Biomater Sci
January 2025
Department of Food Science & Technology, Faculty of Science, National University of Singapore, 117546, Singapore.
Norovirus (NoV) infection is a leading cause of gastroenteritis and poses global health threats, with increasing incidence reported in immunocompromised individuals, which is further exacerbated by the globalization of the food industry. Eumelanin has demonstrated its potential in antiviral treatments, but its role in preventing viral infections remains underexplored. Therefore, in this study, we investigated the antiviral properties and potential mechanisms of self-assembled eumelanin nanoparticles (EmNPs) against Tulane virus (TuV), a surrogate with a similar infection mechanism to NoVs.
View Article and Find Full Text PDFThe structure and assembly of the hetero-octameric BLOC-one-related complex.
Structure
December 2024
Key Laboratory of Biomacromolecules (CAS), National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China; College of Life Sciences, University of Chinese Academy of Sciences, Beijing 100049, China. Electronic address:
BORC (BLOC-one-related complex) is a hetero-octameric complex, consisting of eight coiled-coil proteins (BORCS1-8). BORC controls lysosomal and synaptic vesicle transport and positioning by recruiting ARL8. The structural mechanisms underlying BORC assembly and ARL8 activation remain unclear.
View Article and Find Full Text PDFBmpallidin, encoding a subunit of the BLOC-1 complex, is involved in urate granules formation in silkworm integument.
Int J Biol Macromol
December 2024
Integrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City, Biological Science Research Center, Southwest University, Chongqing 400715, China; Chongqing Engineering and Technology Research Center for Novel Silk Materials, Southwest University, Chongqing 400715, China. Electronic address:
The abnormal development of urate granules in silkworm larvae leads to translucent mutants with a distinct transparent phenotype. Studies on such mutants are expected to enhance current understanding of uric acid metabolism. The hoarfrost translucent (oh) mutant exhibits a mottled, translucent larval integument due to the presence of smaller and irregularly shaped urate granules compared to wild-type individuals.
View Article and Find Full Text PDFA structure-based mechanism for initiation of AP-3 coated vesicle formation.
Proc Natl Acad Sci U S A
December 2024
Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill School of Medicine, Chapel Hill, NC 27599.
Adaptor protein complex-3 (AP-3) mediates cargo sorting from endosomes to lysosomes and lysosome-related organelles. Recently, it was shown that AP-3 adopts a constitutively open conformation compared to the related AP-1 and AP-2 coat complexes, which are inactive until undergoing large conformational changes upon membrane recruitment. How AP-3 is regulated is therefore an open question.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!