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Gamma-aminobutyric acid A receptors [GABA(A) receptors] are ligand-gated chloride channels that mediate inhibitory neurotransmission. Additionally we are shipping GABA(A) Receptor-Associated Protein Antibodies (181) and GABA(A) Receptor-Associated Protein Proteins (24) and many more products for this protein.
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KBTBD6 and KBTBD7 specifically bind to GABARAP proteins.GABARAP proteins mediate localized ubiquitylation of TIAM1 by CUL3 (show CUL3 ELISA Kits).
Data show that WAC (show WAC ELISA Kits) directly binds to GM130 (show GOLGA2 ELISA Kits) and that this binding is required for autophagosome formation through interacting with GABARAP regulating its subcellular localization.
The interaction of GABARAP with Mulan-Ube2E3 supports the role of Mulan as an important regulator of mitophagy.
The FLCN (show FLCN ELISA Kits)-GABARAP association is modulated by the presence of either folliculin (show FLCN ELISA Kits)-interacting protein (FNIP)-1 (show FNIP1 ELISA Kits) or FNIP2 and further regulated by ULK1 (show ULK1 ELISA Kits).
A functional complementation of an lgg-1 null mutant with human GABARAP, its closer homolog showed that it localizes to autophagosomes and can rescue LGG-1 functions in the early embryo.
PLEKHM1 (show PLEKHM1 ELISA Kits) regulates autophagosome-lysosome fusion through homotypic fusion and protein sorting complex and LC3 (show MAP1LC3A ELISA Kits)/GABARAP proteins.
GABARBP dramatically inhibited VEGF (show VEGFA ELISA Kits)-induced endothelial cell proliferation, migration, and tube formation, as well as VEGFR-2 (show KDR ELISA Kits) phosphorylation in vitro.
knockdown of LC3B (show MAP1LC3B ELISA Kits) but not GABARAPs resulted in significant accumulation of p62/Sqstm1 (show SQSTM1 ELISA Kits), one of the selective substrates for autophagy
These results support the regulatory role of Bcl-2 (show BCL2 ELISA Kits) in autophagy and define GABARAP as a novel interaction partner involved in this intricate connection.
Taken together, our results indicate that GABARBP can regulate the pro-apoptotic activity of cisplatin via the upregulation of p53 (show TP53 ELISA Kits) expression.
DLG4/PSD95 (show DLG4 ELISA Kits) and GABARAP were analyzed using zebrafish embryos with morpholino knockdown system as a model organism.
Lipidation of the LC3 (show MAP1LC3A ELISA Kits)/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3 (show ATG3 ELISA Kits).
Results indicate that, compared with LC3 (show MAP1LC3A ELISA Kits), GABARAP is enriched in the axonal initial segments (AIS (show AR ELISA Kits)).
Gabarap functions in the immune system. It is involved in mitochondrial quality control in macrophages, and thus it influences Nlrp3 (show NLRP3 ELISA Kits) inflammasome-dependent inflammatory responses.
ATG8 (show MAP1LC3B ELISA Kits)-like proteins (MAP1LC3B (show MAP1LC3B ELISA Kits), GABARAP and GABARAPL1 (show GABARAPL1 ELISA Kits)) are novel interactors of MAPK15/ERK8 (show MAPK15 ELISA Kits), a MAP kinase (show MAPK1 ELISA Kits) involved in cell proliferation and transformation.
GABARAP/p62 complex is responsible for impairment of glomerular function and that it retards recovery from the effects of doxorubicin.
because of its stronger binding for hKOPR, GEC1 (show GABARAPL1 ELISA Kits) is able to be recruited by hKOPR sufficiently without membrane association via its C-terminal modification; however, du GABARAP appears to require C-terminal modifications to enhance KOPR expression.
In GABARAP-deficient mice renal NaPi-IIa (show SLC34A1 ELISA Kits) is up-regulation and intestinal NaPi-IIb (show SLC34A2 ELISA Kits) is downregulated.
Results suggest that lysosomal turnover of GABARAP-PL is activated during the differentiation of C2C12 cells to myotubes without inactivation of the mTor (show FRAP1 ELISA Kits) kinase-signaling pathway.
the organization of extrasynaptic GABA(A) receptors and GABARAP may provide a range of distinct inhibitory currents in the brain
Gamma-aminobutyric acid A receptors
GABA(A) receptor-associated protein
, gaba(a) receptor-associated protein
, gamma-aminobutyric acid receptor-associated protein
, gamma-aminobutyric acid receptor associated protein
, cerebelluar GABA-A receptor-associated protein
, GABA(A) receptor associated protein
, GABA-A receptor-associated protein
, gamma-aminobutyric acid reseptor associated protein