scholarly journals The Size of Activating and Inhibitory Killer Ig-like Receptor Nanoclusters Is Controlled by the Transmembrane Sequence and Affects Signaling

Cell Reports ◽  
2016 ◽  
Vol 15 (9) ◽  
pp. 1957-1972 ◽  
Author(s):  
Anna Oszmiana ◽  
David J. Williamson ◽  
Shaun-Paul Cordoba ◽  
David J. Morgan ◽  
Philippa R. Kennedy ◽  
...  
Keyword(s):  
Transmembrane Sequence

Structural and Organizational Studies of Soluble Tar-Chewchea Complexes by Electron Microscopy and Image Analysis

1999 ◽  
Vol 5 (S2) ◽  
pp. 1032-1033
Author(s):  
Noreen R. Francis ◽  
Tanvir R. Shaikh ◽  
Mikhail N. Levit ◽  
Linda A. Melanson ◽  
Jeffrey B. Stock ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Leucine Zipper ◽  
Response Regulator ◽  
Organizational Studies ◽  
Flagellar Motor ◽  
Adapter Protein ◽  
General Picture ◽  
Signaling Domain ◽  
Transmembrane Sequence ◽  
Signaling Domains

The transmembrane receptor for aspartate, Tar, in Escherichia coliand Salmonellais representative of a large class of receptors that generates chemotaxis responses by regulating the activity of an associated histidine kinase, CheA. Tar is composed of an Nterminal extracellular ligand-binding domain linked through a transmembrane sequence to a C-terminal signaling domain in the cytoplasm. The isolated cytoplasmic domain of Tar fused to a leucine zipper sequence forms soluble ternary complexes with CheA and an adapter protein, CheW. The isolated complex is biochemically active, has a molecular weight of 1,400,000 Daltons, and includes approximately 28 receptor signaling domains for 2 CheA dimers.Electron microscopy of the complexes indicates well-defined bundles, presumably composed of numerous receptor filaments surrounding a core of CheA dimers and CheW. CheA also interacts with CheY, the response regulator of the bacterial flagellar motor. Immunoelectron microscopy has provided a general picture of the domain organization of the complexes.

scholarly journals Molecular and functional analysis of mouse decay accelerating factor (CD55)

1999 ◽  
Vol 341 (3) ◽  
pp. 821-829 ◽  
Author(s):  
Claire L. HARRIS ◽  
Neil K. RUSHMERE ◽  
B. Paul MORGAN
Keyword(s):  
Northern Blot Analysis ◽  
Transmembrane Protein ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Terminal Sequence ◽  
Decay Accelerating Factor ◽  
Ovary Cells ◽  
Haemolytic Assay ◽  
A Cell ◽  
Transmembrane Sequence

Molecular cloning of mouse decay accelerating factor (DAF; CD55) predicted two forms of the molecule, one transmembrane (TM) and the other glycosylphosphatidylinositol (GPI)-anchored; these are encoded by separate genes termed Daf-GPI and Daf-TM. In the present study several additional isoforms of mouse DAF, generated by alternative splicing from these genes, are described. Northern-blot analysis of RNA and reverse transcriptase-PCR from various tissues indicated that spleen and testis expressed high levels of DAF, which comprised several species. These species were cloned and sequence analysis revealed various novel forms in addition to those previously reported. Two novel forms were derived from the Daf-TM gene but the transmembrane sequence defined previously was replaced by a unique GPI-anchor addition sequence; one clone also had part of the serine/threonine/proline (STP) region deleted. A third clone, encoding a transmembrane protein, was also derived from this gene but the entire STP region was deleted. A fourth clone, derived from the Daf-GPI gene, contained a novel C-terminal sequence, suggestive of a secreted form of the protein. Two DAF cDNAs (TM and GPI-anchored) were stably expressed in Chinese hamster ovary cells. When these cells were attacked with mouse or rat complement and analysed for C3b deposition, DAF-transfected cells had greatly reduced C3b deposition compared with controls. Transfection with DAF also conferred protection from complement in a cell-lysis assay, and a soluble, recombinant form of mouse DAF inhibited complement in a haemolytic assay.

The Conserved Seven-Transmembrane Sequence NP(X)2,3Y of the G-Protein-Coupled Receptor Superfamily Regulates Multiple Properties of the .beta.2-Adrenergic Receptor

Biochemistry ◽  
1995 ◽  
Vol 34 (47) ◽  
pp. 15407-15414 ◽  
Author(s):  
Larry S. Barak ◽  
Luc Menard ◽  
Stephen S. G. Ferguson ◽  
Anne-Marie Colapietro ◽  
Marc G. Caron
Keyword(s):  
G Protein ◽  
Adrenergic Receptor ◽  
G Protein Coupled Receptor ◽  
Transmembrane Sequence ◽  
Beta 2 ◽  
G Protein Coupled

scholarly journals Residue Gln4863within a Predicted Transmembrane Sequence of the Ca2+Release Channel (Ryanodine Receptor) Is Critical for Ryanodine Interaction

2003 ◽  
Vol 278 (51) ◽  
pp. 51557-51565 ◽  
Author(s):  
Ruiwu Wang ◽  
Lin Zhang ◽  
Jeff Bolstad ◽  
Ni Diao ◽  
Cindy Brown ◽  
...  
Keyword(s):  
Ryanodine Receptor ◽  
Release Channel ◽  
Transmembrane Sequence

P3-405: Aβ42-lowering compounds interfere with APP transmembrane sequence dimerization

2010 ◽  
Vol 6 ◽  
pp. S571-S571
Author(s):  
Luise Richter ◽  
Lisa-Marie Munter ◽  
Julia Ness ◽  
Peter W. Hildebrand ◽  
Mangesh Joshi ◽  
...  
Keyword(s):  
Transmembrane Sequence

Model Peptides Uncover the Role of the β-Secretase Transmembrane Sequence in Metal Ion Mediated Oligomerization

2013 ◽  
Vol 135 (51) ◽  
pp. 19354-19361 ◽  
Author(s):  
Lisa M. Munter ◽  
Holger Sieg ◽  
Tobias Bethge ◽  
Filip Liebsch ◽  
Frank S. Bierkandt ◽  
...  
Keyword(s):  
Metal Ion ◽  
Transmembrane Sequence ◽  
Model Peptides

scholarly journals Pre-transmembrane sequence of Ebola glycoprotein

FEBS Letters ◽  
2002 ◽  
Vol 533 (1) ◽  
pp. 47-53 ◽  
Author(s):  
Asier Sáez-Cirión ◽  
Marı́a J Gómara ◽  
Aitziber Agirre ◽  
José L Nieva
Keyword(s):  
Transmembrane Sequence
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