Zobrazeno 1 - 10
of 63
pro vyhledávání: '"Dan Cassel"'
Publikováno v:
PLoS ONE, Vol 12, Iss 12, p e0189659 (2017)
The Arf GTPase-activating protein ArfGAP1 and its brain-specific isoform ArfGAP1B play an important role in neurotransmission. Here we analyzed the distribution of ArfGAP1 in the mouse brain. We found high levels of ArfGAP1 in the mouse dentate gyrus
Externí odkaz:
https://doaj.org/article/b1b0b9d03b184d758ed9122457de3780
Publikováno v:
Molecular Biology of the Cell
A system for controlled trafficking of proteins is based on modifying the streptavidin-binding peptide with trafficking signals and appending it to reporter proteins. Coexpression with streptavidin results in signal masking, which is reversed upon bi
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 71:1328-1334
The heptameric COPI coat (coatomer) plays an essential role in vesicular transport in the early secretory system of eukaryotic cells. While the structures of some of the subunits have been determined, that of the δ-COP subunit has not been reported
Publikováno v:
PLoS ONE, Vol 12, Iss 12, p e0189659 (2017)
PLoS ONE
PLoS ONE
The Arf GTPase-activating protein ArfGAP1 and its brain-specific isoform ArfGAP1B play an important role in neurotransmission. Here we analyzed the distribution of ArfGAP1 in the mouse brain. We found high levels of ArfGAP1 in the mouse dentate gyrus
Publikováno v:
Scientific Reports
The σ1 subunit of the AP-1 clathrin-coated-vesicle adaptor-protein complex is expressed as three isoforms. Tissues express σ1A and one of the σ1B and σ1C isoforms. Brain is the tissue with the highest σ1A and σ1B expression. σ1B-deficiency lea
Autor:
Dan Cassel, Britta Brügger, Fabian Glaser, Irit Pevzner, Felix T. Wieland, Anna Parnis, Jeroen R.P.M. Strating, Lena Lifshitz, Alexia Herrmann
Publikováno v:
Traffic. 13:849-856
COPI vesicles serve for transport of proteins and membrane lipids in the early secretory pathway. Their coat protein (coatomer) is a heptameric complex that is recruited to the Golgi by the small GTPase Arf1. Although recruited en bloc, coatomer can
Autor:
Maria L. Zapp, Zhongzhen Nie, Anne B. Theibert, Masanobu Satake, John M. Logsdon, Richard T. Premont, Dan Cassel, Elspeth A. Bruford, Hiroki Inoue, Paul A. Randazzo, Richard A. Kahn
Publikováno v:
The Journal of Cell Biology
At the FASEB summer research conference on “Arf Family GTPases”, held in Il Ciocco, Italy in June, 2007, it became evident to researchers that our understanding of the family of Arf GTPase activating proteins (ArfGAPs) has grown exponentially in
Publikováno v:
Journal of Biological Chemistry. 283:8564-8572
The interaction of the Arf1-directed GTPase-activating protein ArfGAP1 with the Golgi apparatus depends on motifs in its noncatalytic part that are unstructured in solution but are capable of folding into amphipathic helices in vitro upon interaction
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
Publikováno v:
Molecular Biology of the Cell. 16:4745-4754
The mechanism of AP-1/clathrin coat formation was analyzed using purified adaptor proteins and synthetic liposomes presenting tyrosine sorting signals. AP-1 adaptors recruited in the presence of Arf1·GTP and sorting signals were found to oligomerize