Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Hana Kimura"'
Autor:
Hana Kimura, Kohei Arasaki, Yuki Ohsaki, Toyoshi Fujimoto, Takayuki Ohtomo, Junji Yamada, Mitsuo Tagaya
Publikováno v:
Journal of Lipid Research, Vol 59, Iss 5, Pp 805-819 (2018)
Lipid droplets (LDs) are ubiquitous organelles that contain neutral lipids and are surrounded by a phospholipid monolayer. How proteins specifically localize to the phospholipid monolayer of the LD surface has been a matter of extensive investigation
Externí odkaz:
https://doaj.org/article/03763c1cc20747108800b312df551246
Publikováno v:
Contact, Vol 2 (2019)
During lipid droplet (LD) formation, several key enzymes for neutral lipid biosynthesis, such as acyl-CoA synthetase 3 (ACSL3), translocate from the bilayer of the endoplasmic reticulum membrane or mitochondria-associated membrane to the monolayer su
Externí odkaz:
https://doaj.org/article/fe1a96c6d72e44ac8cdef1e1367e4f80
Publikováno v:
The Journal of Cell Biology
Legionella pneumophila enters cells in a vacuole derived from the plasma membrane, which then sequesters vesicles from the ER in order to support parasite growth and immune evasion. Arasaki et al. now reveal that the Legionella effector DrrA recruits
Autor:
Kohei Arasaki, Junji Yamada, Mitsuo Tagaya, Hana Kimura, Toyoshi Fujimoto, Takayuki Ohtomo, Yuki Ohsaki
Publikováno v:
Journal of Lipid Research, Vol 59, Iss 5, Pp 805-819 (2018)
Lipid droplets (LDs) are ubiquitous organelles that contain neutral lipids and are surrounded by a phospholipid monolayer. How proteins specifically localize to the phospholipid monolayer of the LD surface has been a matter of extensive investigation
Autor:
Yuri Kurosawa, Akitsugu Yamamoto, Hiroki Inoue, Naoshi Dohmae, Kohei Arasaki, Yuichi Wakana, Shigeru Yanagi, Mitsuo Tagaya, Hana Kimura, Naoki Nishida, Haruki Nagashima
Publikováno v:
EMBO reports. 19
In fed cells, syntaxin 17 (Stx17) is associated with microtubules at the endoplasmic reticulum–mitochondria interface and promotes mitochondrial fission by determining the localization and function of the mitochondrial fission factor Drp1. Upon sta
Syntaxin 17 regulates the localization and function of PGAM5 in mitochondrial division and mitophagy
Autor:
Hana Kimura, Hiroki Inoue, Nobutaka Hattori, Tsuyoshi Inoshita, Jinglei Cheng, Mitsuo Tagaya, Naoshi Dohmae, Yuzuru Imai, Kohei Arasaki, Toshiki Amemiya, Yuichi Wakana, Toyoshi Fujimoto, Kahori Shiba-Fukushima, Masashi Sugo, Naohiko Hirota
Publikováno v:
The EMBO journal. 37(21)
PGAM5, a mitochondrial protein phosphatase that is genetically and biochemically linked to PINK1, facilitates mitochondrial division by dephosphorylating the mitochondrial fission factor Drp1. At the onset of mitophagy, PGAM5 is cleaved by PARL, a rh
Syntaxin 17 promotes lipid droplet formation by regulating the distribution of acyl-CoA synthetase 3
Lipid droplets (LDs) are ubiquitous organelles that contain neutral lipids and are surrounded by a phospholipid monolayer. How proteins specifically localize to the phospholipid monolayer of the LD surface has been a matter of extensive investigation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4577250a06eb269f7e81a284713c17ed
Autor:
Akitsugu Yamamoto, Yuichi Wakana, Hana Kimura, Hiroki Inoue, Kohei Arasaki, Mitsuo Tagaya, Chikano Noda, Mitsuru Matsushita
Publikováno v:
Journal of Biological Chemistry. 289:24304-24313
The distribution and morphology of the endoplasmic reticulum (ER) in mammalian cells depend on both dynamic and static interactions of ER membrane proteins with microtubules (MTs). Cytoskeleton-linking membrane protein (CLIMP)-63 is exclusively local
Publikováno v:
Contact. 2:251525641983871
During lipid droplet (LD) formation, several key enzymes for neutral lipid biosynthesis, such as acyl-CoA synthetase 3 (ACSL3), translocate from the bilayer of the endoplasmic reticulum membrane or mitochondria-associated membrane to the monolayer su
Autor:
Kohei Arasaki1,2 karasaki@toyaku.ac.jp, Hana Kimura2, Mitsuo Tagaya2, Roy, Craig R.1 craig.roy@yale.edu
Publikováno v:
Journal of Cell Biology. Nov2018, Vol. 217 Issue 11, p3863-3872. 10p.