scholarly journals The cytoplasmic C-terminal region of the ATP11C variant determines its localization at the polarized plasma membrane

2019 ◽  
Vol 132 (17) ◽  
pp. jcs231720 ◽  
Author(s):  
Masahiro Takayama ◽  
Hiroyuki Takatsu ◽  
Asuka Hamamoto ◽  
Hiroki Inoue ◽  
Tomoki Naito ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Terminal Region

Human Antinuclear Autoantibodies Crossreacting with the Plasma Membrane and the N-Terminal Region of Histone H2B

1987 ◽  
Vol 16 (7) ◽  
pp. 535-547 ◽  
Author(s):  
O. P. Rekvig ◽  
S. Muller ◽  
J. P. Briand ◽  
B. Skogen ◽  
M.H.V. Van Regenmortel
Keyword(s):  
Plasma Membrane ◽  
Terminal Region ◽  
Histone H2b ◽  
Antinuclear Autoantibodies

scholarly journals The 14-3-3 protein interacts directly with the C-terminal region of the plant plasma membrane H(+)-ATPase.

1997 ◽  
Vol 9 (10) ◽  
pp. 1805-1814 ◽  
Author(s):  
T Jahn ◽  
A T Fuglsang ◽  
A Olsson ◽  
I M Brüntrup ◽  
D B Collinge ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Terminal Region ◽  
Plant Plasma Membrane

scholarly journals Structure and function of the CagA oncoprotein from Helicobacter pylori

2014 ◽  
Vol 70 (a1) ◽  
pp. C839-C839
Author(s):  
Toshiya Senda ◽  
Miki Senda ◽  
Takeru Hayashi ◽  
Masanori Hatakeyama
Keyword(s):  
Helicobacter Pylori ◽  
Plasma Membrane ◽  
Structure And Function ◽  
Terminal Region ◽  
Oncogenic Signaling ◽  
Intrinsically Disordered ◽  
Arginine Residues ◽  
Function Relationship ◽  
Structure And Function Relationship ◽  
And Function

CagA is known as a major bacterial virulence determinant from Helicobacter pylori and is critical for gastric cancer. Upon delivery into the gastric epithelial cells, CagA localizes to the inner leaflet of the plasma membrane and promiscuously interacts with host proteins such as PAR1b and SHP2. The CagA-PAR1-SHP2 complex potentiates oncogenic signaling. Biochemical and physicochemical analyses revealed that CagA is comprises a structured N-terminal region (residues 1-876) and an intrinsically disordered C-terminal region (residues 877-1186). To understand the structure and function relationship of CagA, we determined the crystal structure of the N-terminal region (residues 1-876) of CagA [1]. The N-terminal CagA is rich in α-helices and composed of three domains. Domain I (residues 24-221) is linked to domain II (residues 303-644) by a disordered loop with about 80 amino acid residues. Domain II has a basic patch composed of 14 lysine and 2 arginine residues. Biological experiments revealed that the basic patch mediates the CagA-phosphatidylserine interaction to localize the inner face of the plasma membrane. In addition, we found that C-terminal disordered region forms a lariat-like loop by the interaction between NBS (residues 645 - 824) and CBS (residues 998 - 1038) in the disordered C-terminal region. The formation of the lariat-like loop facilitates promiscuous interaction of CagA with target protein such as SHP2.

scholarly journals Novel isoform of syntaxin 1 is expressed in mammalian cells

1997 ◽  
Vol 321 (1) ◽  
pp. 151-156 ◽  
Author(s):  
Mittur N. JAGADISH ◽  
Judy T. TELLAM ◽  
S. Lance MACAULAY ◽  
Keith H. GOUGH ◽  
David E. JAMES ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Amino Acid ◽  
Cdna Clone ◽  
Mammalian Cells ◽  
Transmembrane Domain ◽  
Terminal Region ◽  
Receptor Protein ◽  
Fat Cell ◽  
Syntaxin 1A ◽  
Truncated Protein

Syntaxin 1A has been identified previously as a neural-cell-specific, membrane-anchored receptor protein required for docking and fusion of synaptic vesicles with the presynaptic plasma membrane. Syntaxin 1A consists of 288 amino acid residues including a 265-residue N-terminal region exposed to the cytoplasm and a C-terminal hydrophobic stretch of 23 residues believed to anchor syntaxin to the plasma membrane. Using a human fat-cell library we have isolated a novel cDNA clone of syntaxin 1A containing an insert of 91 bp in codon 226. This insert and subsequent frame shift generated a cDNA that codes for a truncated protein of 260 residues without the C-terminal transmembrane domain characteristic of the syntaxin family. Analysis of the deduced amino acid sequence of the new cDNA clone, termed syntaxin 1C, showed that it was identical for the first 226 residues with the previously described neural syntaxin 1A, and diverged thereafter. The truncated protein lacked the botulinum neurotoxin C cleavage site (Lys253-Ala254), a feature of the syntaxin 1A protein, because of the novel C-terminal domain of 34 residues. The new C-terminal region contained a single cysteine residue and was moderately rich in proline, with three repeats of a PXP motif. The insert occurred within the region encoding the coiled-coil motifs required for interactions with synaptobrevin, α-SNAP (SNAP being soluble N-ethylmaleimide-sensitive factor attachment protein) and n-Sec1/Munc-18 (n-Sec1 being the rat brain homologue of yeast Sec1p and Munc-18 the mammalian homologue of Caenorhabditis elegans unc-18, but five residues outside the domain previously mapped as being required for binding SNAP-25. Interaction studies in vitro suggested that unlike syntaxin 1A, which binds to both Munc-18a and -18b, syntaxin 1C binds only to Munc-18b. The new isoform syntaxin 1C, which might be generated by alternative splicing of the syntaxin 1 gene, was expressed in several human tissues, including brain. Immunoprecipitation and immunoblotting with the monoclonal antibody HPC-1 and a polyclonal antibody raised against a peptide corresponding to the unique C-terminal 35 residues of syntaxin 1C failed to detect syntaxin 1C at the protein level in extracts of muscle, fat or brain.

scholarly journals Activation of Plant Plasma Membrane H+-ATPase by 14-3-3 Proteins Is Negatively Controlled by Two Phosphorylation Sites within the H+-ATPase C-terminal Region

2008 ◽  
Vol 284 (7) ◽  
pp. 4213-4221 ◽  
Author(s):  
Geoffrey Duby ◽  
Wojciech Poreba ◽  
Dominik Piotrowiak ◽  
Krzysztof Bobik ◽  
Rita Derua ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Terminal Region ◽  
Phosphorylation Sites ◽  
Plant Plasma Membrane

The 14-3-3 Protein Interacts Directly with the C-Terminal Region of the Plant Plasma Membrane H + -ATPase

1997 ◽  
Vol 9 (10) ◽  
pp. 1805 ◽  
Author(s):  
Thomas Jahn ◽  
Anja T. Fuglsang ◽  
Anne Olsson ◽  
Ines Maria Bruntrup ◽  
David B. Collinge ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Terminal Region ◽  
Plant Plasma Membrane

Inhibitory Effect of Sucrose on the Plasma Membrane H+ Pump Activity and Possible Involvement of the C-terminal Region in the Sucrose Effect

2000 ◽  
Vol 113 (1) ◽  
pp. 97-102
Author(s):  
Minobu Kasai ◽  
Kyoko Sato ◽  
Tsuyoshi Ono ◽  
Takako Ono ◽  
Kanji Kasai ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Inhibitory Effect ◽  
Terminal Region ◽  
Pump Activity ◽  
Sucrose Effect
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