Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Wei-ke JI"'
Autor:
Jingru Wang, Juan Xiong, Shuhan Zhang, Dongchen Li, Qingzhu Chu, Weiping Chang, Lin Deng, Wei-Ke Ji
Publikováno v:
Cell Discovery, Vol 10, Iss 1, Pp 1-20 (2024)
Abstract Early endosomes (EEs) are crucial in cargo sorting within vesicular trafficking. While cargoes destined for degradation are retained in EEs and eventually transported to lysosomes, recycled cargoes for the plasma membrane (PM) or the Golgi u
Externí odkaz:
https://doaj.org/article/e890f97f05a1422b86871094ff8fb177
Publikováno v:
Contact, Vol 7 (2024)
The Synaptotagmin-like mitochondrial-lipid binding protein (SMP) domain is found in a group of ER-resident lipid transfer proteins that are recruited to membrane contact sites (MCSs) by adaptors. Deciphering the molecular basis underlying the recruit
Externí odkaz:
https://doaj.org/article/d7412d9ef3c748999118c36149c97832
Publikováno v:
Contact, Vol 6 (2023)
While the physical interactions between the Golgi apparatus (Golgi) and lipid droplets (LDs) have been suggested through system-level imaging, the Golgi-LD membrane contact sites (MCSs) remain largely uncharacterized. Here, we show evidence to suppor
Externí odkaz:
https://doaj.org/article/07209d15abbd4808a77c62b191b7b2ed
Publikováno v:
You-qi chuyun, Vol 40, Iss 12, Pp 1365-1369 (2021)
As X80 pipelines are applied in large scale, the safety of long-term service of long-distance oil and gas pipelines has attracted much attention. In order to solve the problem of detecting the inner surface crack defects of pipelines, experimental re
Externí odkaz:
https://doaj.org/article/efec7322e9b54d59b9e155658c097718
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Metabolic rewiring requires the mobilization of fatty acids (FA) from lipid droplets (LDs) at membrane contact sites (MCSs), although the details of FA transfer remain unclear. Here, the authors show that VPS13D and the ESCRT complex remodel LD membr
Externí odkaz:
https://doaj.org/article/03fa235d34f14508a5ddd8c3dd10f798
Publikováno v:
eLife, Vol 4 (2015)
While the dynamin GTPase Drp1 plays a critical role during mitochondrial fission, mechanisms controlling its recruitment to fission sites are unclear. A current assumption is that cytosolic Drp1 is recruited directly to fission sites immediately prio
Externí odkaz:
https://doaj.org/article/386eba9dcc3c4ce5a95a25e7c2a96bd0
Autor:
Qingzhu Chu, Jingru Wang, Yuanjiao Du, Tiantian Zhou, Anbing Shi, Juan Xiong, Wei-Ke Ji, Lin Deng
Publikováno v:
Cell Death & Differentiation. 30:94-110
In metazoans the endoplasmic reticulum (ER) undergoes extensive remodeling during the cell cycle. The endosomal sorting complexes required for transport (ESCRT) protein CHMP7 coordinates ESCRT-III dependent nuclear envelope reformation during mitotic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcdc56c97a63687cfaa398be02de1a8c
https://doi.org/10.1038/s41418-022-01048-2
https://doi.org/10.1038/s41418-022-01048-2
Publikováno v:
Journal of Cell Biology. 222
ER tubules form and maintain membrane contact sites (MCSs) with late endosomes/lysosomes (LE/lys). The molecular composition and cellular functions of these MCSs are poorly understood. Here, we find that Tex2, an SMP domain-containing lipid transfer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f4337e0fdd35640f97bafc8a59f0436c
https://doi.org/10.1083/jcb.202205133
https://doi.org/10.1083/jcb.202205133
Early endosomes (EEs) are central hubs for cargo sorting in vesicular trafficking. Cargoes destined for degradation retain in EEs that are eventually delivered to lysosomes, while recycled cargo destined for the plasma membrane (PM) or to the Golgi a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5fbe7eed1fb1b552485da7b8bf42dfa9
https://doi.org/10.1101/2022.09.30.510409
https://doi.org/10.1101/2022.09.30.510409
ER tubules form and maintain membrane contact sites (MCSs) with late endosomes/lysosomes (LE/lys). The molecular composition and cellular functions of these MCSs are poorly understood. Here we find that Tex2, an SMP domain-containing lipid transfer p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d7f11171ee5925e8dba3bc7231e2d62e
https://doi.org/10.1101/2022.07.12.499833
https://doi.org/10.1101/2022.07.12.499833