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Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia
The duplication of entire genomes has long been recognized as having great potential for evolutionary novelties, but the mechanisms underlying their resolution through gene loss are poorly… Expand
Ultrastructural Organization of Bovine Chromaffin Cell Cortex—Analysis by Cryofixation and Morphometry of Aspects Pertinent to Exocytosis
We have analyzed ultrathin sections from isolated bovine chromaffin cells grown on plastic support, after fast freezing, by quantitative electron microscopy. We determined the size and intracellular… Expand
Glycosylphosphatidyl inositol-anchored proteins and fyn kinase assemble in noncaveolar plasma membrane microdomains defined by reggie-1 and -2.
- C. A. Stuermer, D. Lang, F. Kirsch, M. Wiechers, S. Deininger, H. Plattner
- Biology, Medicine
- Molecular biology of the cell
- 1 October 2001
Using confocal laser scanning and double immunogold electron microscopy, we demonstrate that reggie-1 and -2 are colocalized in < or =0.1-microm plasma membrane microdomains of neurons and… Expand
Identification of reggie-1 and reggie-2 as plasmamembrane-associated proteins which cocluster with activated GPI-anchored cell adhesion molecules in non-caveolar micropatches in neurons.
Neurons are believed to possess plasmalemmal microdomains and proteins analogous to the caveolae and caveolin of nonneuronal cells. Caveolae are plasmalemmal invaginations where activated… Expand
PrPc capping in T cells promotes its association with the lipid raft proteins reggie‐1 and reggie‐2 and leads to signal transduction
- Claudia A. O. Stuermer, Matthias F. Langhorst, +4 authors H. Plattner
- Medicine, Biology
- FASEB journal : official publication of the…
- 1 November 2004
The cellular prion protein (PrPc) resides in lipid rafts, yet the type of raft and the physiological function of PrPc are unclear. We show here that cross‐linking of PrPc with specific antibodies… Expand
Trafficking of the microdomain scaffolding protein reggie-1/flotillin-2.
- M. Langhorst, Alexander Reuter, +4 authors C. A. Stuermer
- Biology, Medicine
- European journal of cell biology
- 18 April 2008
The reggie/flotillin proteins oligomerize and associate into clusters which form scaffolds for membrane microdomains. Besides their localization at the plasma membrane, the reggies/flotillins reside… Expand
Calcium in ciliated protozoa: sources, regulation, and calcium-regulated cell functions.
In ciliates, a variety of processes are regulated by Ca2+, e.g., exocytosis, endocytosis, ciliary beat, cell contraction, and nuclear migration. Differential microdomain regulation may occur by… Expand
Autophagic tubes: vacuolar invaginations involved in lateral membrane sorting and inverse vesicle budding.
Many intracellular compartments of eukaryotic cells do not adopt a spherical shape, which would be expected in the absence of mechanisms organizing their structure. However, little is known about the… Expand
An Ins(1,4,5)P3 receptor in Paramecium is associated with the osmoregulatory system
- E. Ladenburger, I. Korn, N. Kasielke, T. Wassmer, H. Plattner
- Medicine, Biology
- Journal of Cell Science
- 1 September 2006
In the ciliate Paramecium, a variety of well characterized processes are regulated by Ca2+, e.g. exocytosis, endocytosis and ciliary beat. Therefore, among protozoa, Paramecium is considered a model… Expand
Linking membrane microdomains to the cytoskeleton: Regulation of the lateral mobility of reggie‐1/flotillin‐2 by interaction with actin
- M. Langhorst, G. P. Solis, Sylvia Hannbeck, H. Plattner, C. A. Stuermer
- Chemistry, Medicine
- FEBS letters
- 2 October 2007
The reggies/flotillins are oligomeric scaffolding proteins for membrane microdomains. We show here that reggie‐1/flotillin‐2 microdomains are organized along cortical F‐actin in several cell types.… Expand