No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
We have also observed membrane aggregation induced by ATG3 in vitro, which could point to a more complex function of this protein in AP biogenesis. Moreover, in vitro GABARAP lipidation assays suggest that ATG3-membrane interaction could facilitate the lipidation of ATG8 homologues.
These results indicate that GABARAP and PI4K2A interact tightly. Although lipidation of GABARAP is essential for its role in autophagy, here we show that its lipidation is not required for the interaction of GABARAP and PI4K2A.
GABARAPs are identified as the first known direct interaction partners of Nef that are essential for its plasma membrane localization.
GABARAP regulates overall cellular levels of Fn14. Fn14 accumulates in the ERGIC in absence of GABARAP but within endosomes in the vicinity of autophagic membranes in absence of GATE-16.
The centrosome and centriolar satellites regulate autophagosome formation by delivery of an ATG8-family member, GABARAP, to the forming autophagosome membrane, the phagophore. Its proposed that GABARAP regulates phagophore expansion by activating the ULK complex. [review]
GABAergic synapse is proposed as a focus of aging. (Review)
Cardiolipin interaction with various Atg8 human orthologs, namely LC3B, GABARAPL2 and GABARAP, was investigated.
Although neither GABARAPs nor LC3s are required for autophagosome biogenesis, loss of all Atg8s yields smaller autophagosomes and a slowed initial rate of autophagosome formation.
Development of LC3/GABARAP sensors containing a LIR and a hydrophobic domain to monitor autophagy.
GABRP plays an important role in placentation and this pathway may be a promising molecular target for the development of novel therapeutic strategies for preeclampsia.
KBTBD6 and KBTBD7 specifically bind to GABARAP proteins.GABARAP proteins mediate localized ubiquitylation of TIAM1 by CUL3.
Data show that WAC directly binds to GM130 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-GABARAP association is modulated by the presence of either folliculin-interacting protein (FNIP)-1 or FNIP2 and further regulated by ULK1.
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 regulates autophagosome-lysosome fusion through homotypic fusion and protein sorting complex and LC3/GABARAP proteins.
GABARBP dramatically inhibited VEGF-induced endothelial cell proliferation, migration, and tube formation, as well as VEGFR-2 phosphorylation in vitro.
knockdown of LC3B but not GABARAPs resulted in significant accumulation of p62/Sqstm1, one of the selective substrates for autophagy
These results support the regulatory role of Bcl-2 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 expression.
DLG4/PSD95 and GABARAP were analyzed using zebrafish embryos with morpholino knockdown system as a model organism.
Cells that lacked GABARAPs and mice that lacked Gate-16 alone were defective in the IFN-gamma-induced clearance of vacuolar pathogens such as Toxoplasma. GABARAPs are uniquely required for antimicrobial host defense through cytosolic distribution of interferon-inducible GTPases.
Ablation of GABARAP inhibits tumor initiation and progression through enhancement of both antitumor immunity and cell death signaling.
Lipidation of the LC3/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3.
Results indicate that, compared with LC3, GABARAP is enriched in the axonal initial segments (AIS).
Gabarap functions in the immune system. It is involved in mitochondrial quality control in macrophages, and thus it influences Nlrp3 inflammasome-dependent inflammatory responses.
ATG8-like proteins (MAP1LC3B, GABARAP and GABARAPL1) are novel interactors of MAPK15/ERK8, a MAP kinase 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 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 is up-regulation and intestinal NaPi-IIb 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 kinase-signaling pathway.
the organization of extrasynaptic GABA(A) receptors and GABARAP may provide a range of distinct inhibitory currents in the brain
GABARAP binds to and promotes trafficking of the AT(1)R to the plasma membrane.
The expression of Na(+)/H(+) exchanger regulatory factor (NHERF)1, an important scaffold for the apical expression of NaPi-IIa, is also increased in GABARAP(-/-) mice
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