Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Miriam Rotman"'
Autor:
Lior Regev, Anna Parnis, Batya Barkan, Michal Gaitner, Moran Rawet, Dan Cassel, Miriam Rotman
Publikováno v:
Journal of Biological Chemistry. 281:3785-3792
The Arf1-directed GTPase-activating protein ArfGAP1 is a Golgi-localized protein that controls the dynamics of the COPI coat of carriers that mediate transport in the endoplasmic reticulum-Golgi shuttle. Previously the interaction of ArfGAP1 with the
Autor:
Pak P. Poon, Dan Cassel, Miriam Rotman, Richard A. Singer, Elah Pick, Anne Spang, Gerald C. Johnston
Publikováno v:
The EMBO Journal. 18:555-564
ARF proteins, which mediate vesicular transport, have little or no intrinsic GTPase activity. They rely on the actions of GTPase-activating proteins (GAPs) for their function. The in vitro GTPase activity of the Saccharomyces cerevisiae ARF proteins
Autor:
Miriam Rotman, Dan Cassel, Richard A. Singer, Xiangmin Wang, Edna Cukierman, Irit Huber, Pak P. Poon, Gerald C. Johnston
Publikováno v:
Proceedings of the National Academy of Sciences. 93:10074-10077
Movement of material between intracellular compartments takes place through the production of transport vesicles derived from donor membranes. Vesicle budding that results from the interaction of cytoplasmic coat proteins (coatomer and clathrin) with
Publikováno v:
Journal of Biological Chemistry. 270:5232-5237
The small GTP-binding protein ARF plays an established role in the control of vesicular traffic and in the regulation of phospholipase D activity. Like other GTP binding proteins, ARF becomes activated upon the binding of GTP, whereas GTP hydrolysis
Publikováno v:
Experimental Parasitology. 72:411-417
We investigated the presence in Leishmania donovani promastigotes of proteins with homology to the G-proteins known to mediate signal transduction in other organisms. [alpha 32P]GTP binding experiments revealed the presence in the promastigote membra
Regulators of Arf activity include a family of proteins with a shared domain, the cysteine-rich Arf GAP domain, that is responsible for activating the latent GTPase activity of Arfs. The first of these to be discovered, Arf GAP1 is the focus of this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3f7c4a1920c3cde02918afaa56cfc7ca
https://doi.org/10.1385/1-59259-281-3:199
https://doi.org/10.1385/1-59259-281-3:199
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 189
Publikováno v:
The Journal of biological chemistry. 276(51)
The interaction of the coatomer coat complex with the Golgi membrane is initiated by the active, GTP-bound state of the small GTPase ADP-ribosylation factor 1 (ARF1), whereas GTP hydrolysis triggers coatomer dissociation. The hydrolysis of GTP on ARF
This chapter describes the expression, purification, and properties of adenosine diphopshate (ADP)-ribosylation factor (ARF) guanosine triphosphate (GTP)ase activating protein-1(GAP1). GAP1 is expressed at low level, comprising less than 0.01% of cyt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::51937f11daea174fb63ec68a85cf8364
https://doi.org/10.1016/s0076-6879(01)29092-2
https://doi.org/10.1016/s0076-6879(01)29092-2
Publikováno v:
The Journal of biological chemistry. 275(31)
The binding of the coat protein complex, coatomer, to the Golgi is mediated by the small GTPase ADP-ribosylation factor-1 (ARF1), whereas the dissociation of coatomer, requires GTP hydrolysis on ARF1, which depends on a GTPase-activating protein (GAP