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4 results on '"Ravdandorj, Odongoo"'

2. Functional role of c-Jun NH2-terminal kinase-associated leucine zipper protein (JLP) in lysosome localization and autophagy

Author

Katsuji Yoshioka, Purev Erdenebaatar, Ryusuke Suzuki, Jambaldorj Boldbaatar, Ravdandorj Odongoo, and I Ketut Gunarta

Subjects
Lysosomal transport, 0303 health sciences, Leucine zipper, Chemistry, Dynein, Autophagy, Lysosome localization, General Medicine, Transmembrane protein, Cell biology, 03 medical and health sciences, 0302 clinical medicine, 030220 oncology & carcinogenesis, Dynactin, Kinesin, Pharmacology (medical), General Pharmacology, Toxicology and Pharmaceutics, 030304 developmental biology
Abstract

Lysosomes are involved in many cellular functions, and in turn lysosomal dysfunction underlies a variety of diseases, including cancer and neurodegenerative diseases. Lysosomes are distributed broadly in the cytoplasm and can move throughout the cell in kinesin- and dynein-dependent manners. Although many mechanisms of lysosomal transport have been reported, how lysosomal transport is regulated has yet to be fully elucidated. In this study we analyzed c-Jun NH2-terminal kinase-associated leucine zipper protein (JLP), an adaptor of kinesin and dynein motor proteins, and found that lysosomes were localized toward the cell periphery in JLP knockdown cells, leading to the impairment of autophagosome-lysosome fusion. Furthermore, we performed rescue experiments using wild-type JLP and its various deletion mutants. The results indicated that JLP may regulate lysosome localization and autophagy through interaction of JLP with kinesin-1 heavy chain, but not with dynactin p150Glued or lysosomal transmembrane protein 55b. Our findings provide new insights into the mechanisms of lysosomal trafficking regulation. This study contributes to the understanding of how lysosomes exert their multiple functions, potentially leading to the identification of molecular targets for diseases caused by lysosomal dysfunction.

Published
2020
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3. Functional role of c-Jun NH

Author

Ryusuke, Suzuki, I Ketut, Gunarta, Jambaldorj, Boldbaatar, Purev, Erdenebaatar, Ravdandorj, Odongoo, and Katsuji, Yoshioka

Subjects
Autophagy, Humans, Kinesins, Mitogen-Activated Protein Kinase 9, Dynactin Complex, Lysosomes, Adaptor Proteins, Signal Transducing
Abstract

Lysosomes are involved in many cellular functions, and in turn lysosomal dysfunction underlies a variety of diseases, including cancer and neurodegenerative diseases. Lysosomes are distributed broadly in the cytoplasm and can move throughout the cell in kinesin- and dynein-dependent manners. Although many mechanisms of lysosomal transport have been reported, how lysosomal transport is regulated has yet to be fully elucidated. In this study we analyzed c-Jun NH

Published
2020

4. c-Jun NH2-terminal kinase (JNK)/stress-activated protein kinase-associated protein 1 (JSAP1) attenuates curcumin-induced cell death differently from its family member, JNK-associated leucine zipper protein (JLP).

Author

Gunarta, I. Ketut, Dewi Yuliana, Purev Erdenebaatar, Yuhei Kishi, Jambaldorj Boldbaatar, Ryusuke Suzuki, Ravdandorj Odongoo, Gantulga Davaakhuu, Hirohiko Hohjoh, and Katsuji Yoshioka

Subjects
*LEUCINE zippers, *CELL death, *SCAFFOLD proteins, *MITOGEN-activated protein kinases, *SMALL molecules
Abstract

Curcumin, a major component of turmeric, is known to exhibit multiple biological functions including antitumor activity. We previously reported that the mitogen-activated protein kinase (MAPK) scaffold protein c-Jun NH2-terminal kinase (JNK)-associated leucine zipper protein (JLP) reduces curcumininduced cell death by modulating p38 MAPK and autophagy through the regulation of lysosome positioning. In this study, we investigated the role of JNK/stress-activated protein kinase-associated protein 1 (JSAP1), a JLP family member, in curcumin-induced stress, and found that JSAP1 also attenuates curcumin-induced cell death. However, JSAP1 knockout showed no or little effect on the activation of JNK and p38 MAPKs in response to curcumin. In addition, small molecule inhibitors of JNK and p38 MAPKs did not increase curcumin-induced cell death. Furthermore, JSAP1 depletion did not impair lysosome positioning and autophagosome-lysosome fusion. Instead, we noticed substantial autolysosome accumulation accompanied by an inefficient autophagic flux in JSAP1 knockout cells. Taken together, these results indicate that JSAP1 is involved in curcumin-induced cell death differently from JLP, and may suggest that JSAP1 plays a role in autophagosome degradation and its dysfunction results in enhanced cell death. The findings of this study may contribute to the development of novel therapeutic approaches using curcumin for cancer. [ABSTRACT FROM AUTHOR]

Published
2021
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