Properties of γ-Aminobutyric Acid Receptor/Ionophore Proteins from Crayfish Muscle

1977 ◽  
Vol 5 (4) ◽  
pp. 863-866 ◽  
Author(s):  
RICHARD W. OLSEN ◽  
BRAD MEINERS ◽  
PAT KEHOE ◽  
MAHARAJ K. TICKU
Keyword(s):  
Aminobutyric Acid ◽  
Acid Receptor ◽  
Crayfish Muscle

?-AMINOBUTYRIC ACID RECEPTOR BINDING and UPTAKE IN MEMBRANE FRACTIONS OF CRAYFISH MUSCLE

1979 ◽  
Vol 32 (3) ◽  
pp. 979-990 ◽  
Author(s):  
B. M. Meiners ◽  
P. Kehoe ◽  
D. M. Shaner ◽  
R. W. Olsen
Keyword(s):  
Receptor Binding ◽  
Aminobutyric Acid ◽  
Acid Receptor ◽  
Crayfish Muscle

Two ubiquitin-like conjugation systems that mediate membrane formation during autophagy

2013 ◽  
Vol 55 ◽  
pp. 39-50 ◽  
Author(s):  
Hitoshi Nakatogawa
Keyword(s):  
Light Chain ◽  
Membrane Dynamics ◽  
The Other ◽  
Aminobutyric Acid ◽  
Amino Group ◽  
Autophagosome Formation ◽  
Acid Receptor ◽  
Receptor Associated Protein ◽  
Atg Proteins ◽  
C Terminus

In autophagy, the autophagosome, a transient organelle specialized for the sequestration and lysosomal or vacuolar transport of cellular constituents, is formed via unique membrane dynamics. This process requires concerted actions of a distinctive set of proteins named Atg (autophagy-related). Atg proteins include two ubiquitin-like proteins, Atg12 and Atg8 [LC3 (light-chain 3) and GABARAP (γ-aminobutyric acid receptor-associated protein) in mammals]. Sequential reactions by the E1 enzyme Atg7 and the E2 enzyme Atg10 conjugate Atg12 to the lysine residue in Atg5, and the resulting Atg12–Atg5 conjugate forms a complex with Atg16. On the other hand, Atg8 is first processed at the C-terminus by Atg4, which is related to ubiquitin-processing/deconjugating enzymes. Atg8 is then activated by Atg7 (shared with Atg12) and, via the E2 enzyme Atg3, finally conjugated to the amino group of the lipid PE (phosphatidylethanolamine). The Atg12–Atg5–Atg16 complex acts as an E3 enzyme for the conjugation reaction of Atg8; it enhances the E2 activity of Atg3 and specifies the site of Atg8–PE production to be autophagy-related membranes. Atg8–PE is suggested to be involved in autophagosome formation at multiple steps, including membrane expansion and closure. Moreover, Atg4 cleaves Atg8–PE to liberate Atg8 from membranes for reuse, and this reaction can also regulate autophagosome formation. Thus these two ubiquitin-like systems are intimately involved in driving the biogenesis of the autophagosomal membrane.

Deficiency of the β3 subunit of the type A γ–aminobutyric acid receptor causes cleft palate in mice

1995 ◽  
Vol 11 (3) ◽  
pp. 344-346 ◽  
Author(s):  
Cymbeline T. Culiat ◽  
Lisa J. Stubbs ◽  
Richard P. Woychik ◽  
Liane B. Russell ◽  
Dabney K. Johnson ◽  
...  
Keyword(s):  
Cleft Palate ◽  
Type A ◽  
Aminobutyric Acid ◽  
Acid Receptor

scholarly journals Synthesis, Anticonvulsant Evaluation and Molecular Docking Studies of Novel Benzo[1,3]dioxol-5-yloxy-N′-(4-substituted benzylidene)acetohydrazide Derivatives

2019 ◽  
Vol 32 (1) ◽  
pp. 199-204
Author(s):  
Shailesh Kumar Singh ◽  
Laxmi Tripathi
Keyword(s):  
Molecular Docking ◽  
Mechanism Of Action ◽  
Anticonvulsant Activity ◽  
Docking Studies ◽  
Probable Mechanism ◽  
Aminobutyric Acid ◽  
Docking Score ◽  
Acid Receptor ◽  
Seizure Models ◽  
Gabaergic Activity

Novel (benzo[1,3]dioxol-5-yloxy)-N′-(4-substituted benzylidene)acetohydrazide derivatives were synthesized and their anticonvulsant activity evaluated by MES and scMET seizure models. Compound 2-(benzo[d][1,3]dioxol-5-yloxy)-N′-benzylideneacetohydrazide (4a) was found to be most potent in MES seizure test and showed no neurotoxicity at the highest administered dose. All the compounds showed high docking score with γ-aminobutyric acid receptor, GABAAR-β3 homopentamer (PDB ID: 4COF). Thus, the probable mechanism of action of benzo[1,3]dioxol-5-yloxy-N′-(4-substituted benzylidene)acetohydrazide derivatives (4a-h) may be augmentation of GABAergic activity.

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