Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Tomohiro Yorimitsu"'
Publikováno v:
PLoS ONE, Vol 7, Iss 7, p e40765 (2012)
Although it is well established that the coat protein complex II (COPII) mediates the transport of proteins and lipids from the endoplasmic reticulum (ER) to the Golgi apparatus, the regulation of the vesicular transport event and the mechanisms that
Externí odkaz:
https://doaj.org/article/d9db15bb229f48609caf5794703d1176
Autor:
Tomohiro Yorimitsu, Ken Sato
Publikováno v:
Journal of Cell Science. 136
COPII proteins assemble at ER exit sites (ERES) to form transport carriers. The initiation of COPII assembly in the yeast Saccharomyces cerevisiae is triggered by the ER membrane protein Sec12. Sec16, which plays a critical role in COPII organization
Autor:
Ken Sato, Tomohiro Yorimitsu
Publikováno v:
Molecular Biology of the Cell. 31:149-156
COPII components undergo phosphorylation to drive ER export and autophagy. Here we found that the nonphosphorylatable Sec16 mutant exhibits no defect in ER export and autophagy. Our findings indicate that in Saccharomyces cerevisiae, Sec16 phosphoryl
Publikováno v:
Cell Structure and Function. 44:105-112
The coat protein complex II (COPII) generates transport carriers that deliver newly synthesized proteins from the endoplasmic reticulum (ER) to the Golgi apparatus. The small GTPase Sar1 is a well-known regulator of the assembly of the COPII coat. In
Autor:
Tomohiro, Yorimitsu, Ken, Sato
Publikováno v:
Molecular Biology of the Cell
Coat protein complex II (COPII) protein assembles at the endoplasmic reticulum exit site (ERES) to form vesicle carrier for transport from the ER to the Golgi apparatus. Sec16 has a critical role in COPII assembly to form ERES. Sec16∆565N mutant, w
Autor:
Norito Sasaki, Ken Sato, Miharu Maeda, Kota Saito, Tomohiro Yorimitsu, Toshiaki Katada, Masano Shiraiwa
Secretory proteins synthesized within the endoplasmic reticulum (ER) are exported via coat protein complex II (COPII)-coated vesicles. The formation of the COPII-coated vesicles is initiated by activation of the small GTPase, Sar1. cTAGE5 directly in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24d90793463b6f67617690b0e649b0cf
Autor:
Aisa Sakaguchi, Miyuki Sato, Katsuya Sato, Keiko Gengyo-Ando, Tomohiro Yorimitsu, Junichi Nakai, Taichi Hara, Ken Sato
Publikováno v:
Developmental Cell. 35(2):211-221
SummaryThe small GTPase Rab11 dynamically changes its location to regulate various cellular processes such as endocytic recycling, secretion, and cytokinesis. However, our knowledge of its upstream regulators is still limited. Here, we identify the R
Publikováno v:
FEBS Letters. 589:1234-1239
COPII vesicles are formed at specific subdomains of the ER, termed ER exit sites (ERESs). Depending on the cell type, ERESs number from a few to several hundred per cell. However, whether these ERESs are functionally and compositionally identical at
Publikováno v:
Journal of Cell Science.
COPII coat and the small GTPase Sar1 mediate protein export from the endoplasmic reticulum (ER) via specialized domains known as the ER exit sites. The peripheral ER protein Sec16 has been proposed to organize ER exit sites. However, it remains uncle
Publikováno v:
Molecular Biology of the Cell. 18:4180-4189
Autophagy is a highly conserved, degradative process in eukaryotic cells. The rapamycin-sensitive Tor kinase complex 1 (TORC1) has a major role in regulating induction of autophagy; however, the regulatory mechanisms are not fully understood. Here, w