Zobrazeno 1 - 10
of 79
pro vyhledávání: '"Thomas E. Kreis"'
Autor:
Silvia Martin-Lluesma, Bruno Goud, Sandrine Moutel, Franck Perez, Thomas E. Kreis, Aurélien Roux, Clément Nizak
Publikováno v:
Traffic. 4:739-753
Generation of specific antibodies against enriched subcellular fractions is a powerful strategy to identify and characterize cellular components. We show that recombinant antibodies can be selected in vitro by phage display against complex subcellula
Autor:
M. Josh Hasbani, Thomas E. Kreis, Michael Schrader, Trina A. Schroer, Dawn M. Wetzel, Steven R. Gill, Caterina Valetti
Publikováno v:
Molecular Biology of the Cell. 10:4107-4120
The flow of material from peripheral, early endosomes to late endosomes requires microtubules and is thought to be facilitated by the minus end-directed motor cytoplasmic dynein and its activator dynactin. The microtubule-binding protein CLIP-170 may
Autor:
Ronald Melki, Georgios S. Diamantopoulos, Thomas E. Kreis, Janet E. Rickard, Holly V. Goodson, Gérard Batelier, Franck Perez
Publikováno v:
The Journal of Cell Biology
CLIP-170 is a cytoplasmic linker protein that localizes to plus ends of microtubules in vivo. In this study, we have characterized the microtubule-binding properties of CLIP-170, to understand the mechanism of its plus end targeting. We show that the
Autor:
Thomas E. Kreis, Martin Lowe
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1404:53-66
Intracellular membrane transport is mediated predominantly by vesicles which bud from one compartment and fuse specifically with the next compartment in the pathway, resulting in delivery of cargo. COPI-coated vesicles were first identified as interm
Autor:
Anne Moreau, Jan R. De Mey, Thomas E. Kreis, Suzie J. Scales, Dagmar Hennig, Laura Lea Murley
Publikováno v:
Journal of Biological Chemistry. 273:19602-19611
A protein of 60 kDa (p60) has been identified using a quantitative in vitro vesicle-microtubule binding assay. Purified p60 induces co-sedimentation with microtubules of trans-Golgi network-derived vesicles isolated from polarized, perforated Madin-D
Publikováno v:
The Journal of Cell Biology
Recent evidence has suggested that subunits of the coatomer protein (COPI) complexes are functionally associated with endosomes in mammalian cells. We now provide genetic evidence that COPI plays a role in endocytosis in intact cells. The ldlF mutant
Publikováno v:
Cell. 90:1137-1148
Exocytic transport from the endoplasmic reticulum (ER) to the Golgi complex has been visualized in living cells using a chimera of the temperature-sensitive glycoprotein of vesicular stomatitis virus and green fluorescent protein (ts-G-GFPct). Upon s
Publikováno v:
Current Opinion in Cell Biology. 9:18-28
The cytoskeleton is essential for the proper function of many components of secretory and endocytic pathways, and the importance both of microtubule motors (kinesins and dyneins) and of actin motors (myosins) in these pathways is becoming apparent. R
Publikováno v:
The Journal of Cell Biology
Addition of brefeldin A (BFA) to mammalian cells rapidly results in the removal of coatomer from membranes and subsequent delivery of Golgi enzymes to the endoplasmic reticulum (ER). Microinjected anti-EAGE (intact IgG or Fab-fragments), antibodies a
Autor:
Brian Storrie, Thomas E. Kreis
Publikováno v:
Trends in Cell Biology. 6:321-324
Studies using a variety of microscopy-based approaches have led to a consensus that most cell-surface proteins are highly mobile and diffuse rapidly within fenced microdomains. Little attention, however, has so far been given to the analysis of the m