Zobrazeno 1 - 10
of 92
pro vyhledávání: '"William A. Prinz"'
Autor:
Amit S. Joshi, Benjamin Nebenfuehr, Vineet Choudhary, Prasanna Satpute-Krishnan, Tim P. Levine, Andy Golden, William A. Prinz
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Lipid droplets (LDs) and peroxisomes are both generated by budding off the endoplasmic reticulum (ER). Here, the authors show that the yeast protein Pex30 marks ER subdomains where both LD and peroxisome biogenesis occurs, and identify MCTP2 as the p
Externí odkaz:
https://doaj.org/article/a1e2c94e0d0c4f8b9fcf9587d37bfc71
Publikováno v:
Journal of Lipid Research, Vol 58, Iss 3, Pp 553-562 (2017)
Close contacts between organelles, often called membrane contact sites (MCSs), are regions where lipids are exchanged between organelles. Here, we identify a novel mechanism by which cells promote phospholipid exchange at MCSs. Previous studies have
Externí odkaz:
https://doaj.org/article/0efbd7b7677e45d591c5690c80728960
Autor:
Matthew J Hayes, Vineet Choudhary, Namrata Ojha, John JH Shin, Gil-Soo Han, George M. Carman, Christopher JR Loewen, William A Prinz, Timothy P Levine
Publikováno v:
Microbial Cell, Vol 5, Iss 2, Pp 88-103 (2017)
Fat storage-inducing transmembrane (FIT or FITM) proteins have been implicated in the partitioning of triacylglycerol to lipid droplets and the budding of lipid droplets from the ER. At the molecular level, the sole relevant interaction is that FITMs
Externí odkaz:
https://doaj.org/article/5c562e39cddf446a865bb58729b27306
Autor:
Craig Blackstone, William A Prinz
Publikováno v:
eLife, Vol 5 (2016)
Three proteins work together to control the shape of the endoplasmic reticulum in animal cells.
Externí odkaz:
https://doaj.org/article/9875392221ae44e4a35ebf659d7292aa
Publikováno v:
Microbial Cell, Vol 7, Iss 8, Pp 218-221 (2020)
The Journal of Cell Biology
Microbial Cell
Journal of Cell Biology
The Journal of Cell Biology
Microbial Cell
Journal of Cell Biology
Choudhary et al. show lipid droplet (LD) biogenesis from discrete ER subdomains in yeast. Fld1 together with Nem1 localize to discrete ER subdomains independent of each other and of LDs, but both are required to recruit triacylglycerol (TAG)-synthase
Autor:
Alexandre Toulmay, Fawn B. Whittle, Jerry Yang, Xiaofei Bai, Jessica Diarra, Subhrajit Banerjee, Tim P. Levine, Andy Golden, William A. Prinz
Publikováno v:
Journal of Cell Biology. 221
Glycosylphosphatidylinositol (GPI) is a glycolipid membrane anchor found on surface proteins in all eukaryotes. It is synthesized in the ER membrane. Each GPI anchor requires three molecules of ethanolamine phosphate (P-Etn), which are derived from p
Publikováno v:
Molecular Biology of the Cell
Lipid droplets (LDs) are neutral lipid-containing organelles enclosed in a single monolayer of phospholipids. LD formation begins with the accumulation of neutral lipids within the bilayer of the endoplasmic reticulum (ER) membrane. It is not known h
Autor:
William A. Prinz, Karin M. Reinisch
Publikováno v:
The Journal of Cell Biology
Reinisch and Prinz review the emerging understanding of the mechanisms, regulation, and functions of nonvesicular lipid transport in eukaryotic cells.
We have long known that lipids traffic between cellular membranes via vesicles but have only r
We have long known that lipids traffic between cellular membranes via vesicles but have only r
Autor:
Raunaq A. Deo, William A. Prinz
Publikováno v:
Cell. 184:3591-3592
ESCRT-III proteins, which form filaments that deform, bud, and sever membranes, are found in eukaryotes and some archaea. Three studies in this issue of Cell reveal that PspA and Vipp1 are bacterial and cyanobacterial members of the ESCRT-III superfa
Autor:
Wei Sheng, Yap, Peter, Shyu, Maria Laura, Gaspar, Stephen A, Jesch, Charlie, Marvalim, William A, Prinz, Susan A, Henry, Guillaume, Thibault
Publikováno v:
J Cell Sci
Lipid droplets (LDs) are implicated in conditions of lipid and protein dysregulation. The fat storage-inducing transmembrane (FIT; also known as FITM) family induces LD formation. Here, we establish a model system to study the role of the Saccharomyc