Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Joji Mima"'
Autor:
Kana Fujibayashi, Joji Mima
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 9 (2021)
Arf-family small GTPases are essential protein components for membrane trafficking in all eukaryotic endomembrane systems, particularly during the formation of membrane-bound, coat protein complex-coated transport carriers. In addition to their roles
Externí odkaz:
https://doaj.org/article/6945c6cad5b24adf81d3541fdd59c207
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 8 (2020)
Membrane tethering is a crucial step to determine the spatiotemporal specificity of secretory and endocytic trafficking pathways in all eukaryotic endomembrane systems. Recent biochemical studies by a chemically-defined reconstitution approach reveal
Externí odkaz:
https://doaj.org/article/33a358bc83564272a4c0725fadb9d3d7
Autor:
Naoki Tamura, Joji Mima
Publikováno v:
Biology Open, Vol 3, Iss 11, Pp 1108-1115 (2014)
Rab GTPases are master regulators of eukaryotic endomembrane systems, particularly functioning in membrane tethering to confer the directionality of intracellular membrane trafficking. However, how exactly Rab GTPases themselves act upon membrane tet
Externí odkaz:
https://doaj.org/article/af95a5d29e184dd9842a69161395514d
Autor:
Terry L Bennett, Shannon M Kraft, Barbara J Reaves, Joji Mima, Kevin M O'Brien, Vincent J Starai
Publikováno v:
PLoS ONE, Vol 8, Iss 2, p e56798 (2013)
During infection, the intracellular pathogenic bacterium Legionella pneumophila causes an extensive remodeling of host membrane trafficking pathways, both in the construction of a replication-competent vacuole comprised of ER-derived vesicles and pla
Externí odkaz:
https://doaj.org/article/8da655e7640441a7b3b106c1b89b1cf2
Autor:
Joji Mima
Publikováno v:
Biophys Rev
Small GTPases of the Ras superfamily, which include Ras-, Rho-, Rab-, Arf-, and Ran-family isoforms, are generally known to function as a nucleotide-dependent molecular switch in eukaryotic cells. In the GTP-loaded forms, they selectively recruit the
Publikováno v:
Protein Sci
In macroautophagy, de novo formation of the double membrane-bound organelles, termed autophagosomes, is essential for engulfing and sequestering the cytoplasmic contents to be degraded in the lytic compartments such as vacuoles and lysosomes. Atg8-fa
Autor:
Joji Mima, Kana Fujibayashi
Publikováno v:
Frontiers in Cell and Developmental Biology
Frontiers in Cell and Developmental Biology, Vol 9 (2021)
Frontiers in Cell and Developmental Biology, Vol 9 (2021)
Arf-family small GTPases are essential protein components for membrane trafficking in all eukaryotic endomembrane systems, particularly during the formation of membrane-bound, coat protein complex-coated transport carriers. In addition to their roles
Gatekeeper helix activates Golgi SM protein Sly1 and directly mediates close-range vesicle tethering
Autor:
B. M. Delgado, Rachael L. Plemel, Joji Mima, Una Nattermann, Mengtong Duan, Elizabeth A. Miller, Alexey J. Merz, Daniel P. Nickerson, T. Takenaka, A. Lin
The essential Golgi protein Sly1 is a member of the SM (Sec1/mammalian Unc-18) family of SNARE chaperones. Sly1 was originally identified through gain-of-function alleles that bypass requirements for diverse vesicle tethering factors. Employing genet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59a634574df040a47f697b8a5d5d9717
Autor:
Joji Mima
Publikováno v:
Biophysical Reviews. 10:543-549
Membrane tethering is one of the most critical steps to determine the spatiotemporal specificity of membrane trafficking, which is the process to selectively transport proteins, lipids, and other biological molecules to the appropriate locations in e
Membrane tethering is a highly regulated event that occurs during the initial physical contact between membrane-bounded transport carriers and their target subcellular membrane compartments, thereby ensuring the spatiotemporal specificity of intracel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04009f074e07504238a01c45e34e9fe2