Results 11 to 20 of about 7,891 (186)

Conserved LIR-specific interaction of Sigma-1 receptor and GABARAP [PDF]

iScience
Summary: Among its various functions, the sigma-1 receptor (σ1R) has been reported to modulate macroautophagy. It is currently unknown how this activity is mediated. We phylogenetically, structurally, and biochemically analyzed σ1R regarding its function
Marius Wilhelm Baeken, Maximilian Christ, Daniel Schmitt, Wencke Trein, Heike Nagel, Albrecht Martin Clement, Hagen Körschgen, Christian Behl   +7 more
doaj   +8 more sources

Enrichment of GABARAP relative to LC3 in the axonal initial segments of neurons.

PLoS ONE, 2013
GABAA receptor-associated protein (GABARAP) was initially identified as a protein that interacts with GABAA receptor. Although LC3 (microtubule-associated protein 1 light chain 3), a GABARAP homolog, has been localized in the dendrites and cell bodies of
Masato Koike, Isei Tanida, Tomohisa Nanao, Norihiro Tada, Jun-ichi Iwata, Takashi Ueno, Eiki Kominami, Yasuo Uchiyama   +7 more
doaj   +5 more sources

Critical assessment of LC3/GABARAP ligands used for degrader development and ligandability of LC3/GABARAP binding pockets [PDF]

Nature Communications
Recent successes in developing small molecule degraders that act through the ubiquitin system have spurred efforts to extend this technology to other mechanisms, including the autophagosomal-lysosomal pathway.
Martin P. Schwalm, Johannes Dopfer, Adarsh Kumar, Francesco A. Greco, Nicolas Bauer, Frank Löhr, Jan Heering, Sara Cano-Franco, Severin Lechner, Thomas Hanke, Ivana Jaser, Viktoria Morasch, Christopher Lenz, Daren Fearon, Peter G. Marples, Charles W. E. Tomlinson, Lorene Brunello, Krishna Saxena, Nathan B. P. Adams, Frank von Delft, Susanne Müller, Alexandra Stolz, Ewgenij Proschak, Bernhard Kuster, Stefan Knapp, Vladimir V. Rogov   +25 more
doaj   +6 more sources

GABARAP and GABAA Receptor Clustering [PDF]

Neuron, 2002
Coyle et al. (2002), in this issue of Neuron, reveal the crystal structure for the GABA(A) receptor binding protein, GABARAP. They show GABARAP can switch from a monomer to an extended linear polymer form that may function to assemble microtubules during the intracellular trafficking or postsynaptic clustering of GABA(A) receptors.
Phillips, William D., Froehner, Stanley C.   +1 more
openaire   +4 more sources

The highly GABARAP specific rat monoclonal antibody 8H5 visualizes GABARAP in immunofluorescence imaging at endogenous levels [PDF]

Scientific Reports, 2019
Abstract The determination of unique functions of GABARAP (gamma-aminobutyric acid type A receptor-associated protein), a member of the highly conserved protein family of mammalian autophagy-related 8 protein (mATG8), within diverse cellular processes remains challenging.
Indra M. Simons, Jeannine Mohrlüder, Regina Feederle, Elisabeth Kremmer, Thomas Zobel, Jochen Dobner, Nicole Bleffert, Silke Hoffmann, Dieter Willbold   +8 more
openaire   +5 more sources

Ceramide and the membrane-fusion activity of LC3/GABARAP autophagy proteins [PDF]

Cellular and Molecular Life Sciences
Macroautophagy is a cellular degradation process characterized by the formation of the double-membrane structure termed autophagosome (AP). The process of AP formation is not fully understood, but it is thought to happen through the combined action of ...
Yaiza R. Varela, Camila C. Aguirre, Marina N. Iriondo, Uxue Ballesteros, M. Isabel Collado, Asier Etxaniz, L. Ruth Montes, Felix M. Goñi, Alicia Alonso   +8 more
doaj   +5 more sources

Structural characterization of GABARAP–ligand interactions

Molecular BioSystems, 2009
Abstract The GABAAreceptor-associated protein (GABARAP) plays an important role in intracellular trafficking of several proteins. It undergoes a C-terminal lipidation process that enables anchoring in the cytosolic leaflet of cellular membranes.
Yvonne, Thielmann, Oliver H, Weiergräber, Jeannine, Mohrlüder, Dieter, Willbold   +3 more
openaire   +3 more sources

Crystal structure of the GABAA‐receptor‐associated protein, GABARAP [PDF]

The EMBO Reports, 2002
The GABA(A)-receptor-associated protein (GABARAP) is a member of a growing family of intracellular membrane trafficking and/or fusion proteins and has been implicated in plasma membrane targeting and/or recycling of GABA(A) receptors. GABARAP is localized on intracellular membranes such as the trans-Golgi network, binds to the gamma 2 subunit of GABA(A)
Bavro, V., Sola, M., Bracher, A., Kneussel, M., Betz, H., Weissenhorn, W.   +5 more
openaire   +5 more sources

The sigma-1 receptor as a neurohomeostatic decision hub for GABARAP-mediated receptor trafficking and macroautophagy [PDF]

Frontiers in Molecular Biosciences
Gamma-aminobutyric acid receptor-associated protein (GABARAP) is a multifunctional member of the autophagy-related (ATG8) protein family, playing key roles in two distinct cellular pathways: macroautophagy and plasma membrane protein trafficking.
Marius Wilhelm Baeken, Fazilet Bekbulat, Hagen Körschgen, Albrecht Martin Clement, Christian Behl   +4 more
doaj   +2 more sources

Bioorthogonal Tools for Ethanolamine Lipids and Protein Conjugates. [PDF]

Angew Chem Int Ed Engl
An alkyne‐tagged ethanolamine analog (AlkEA) enables bioorthogonal, metabolic labeling of endogenous phosphatidylethanolamine (PE) and its protein modifications. AlkEA is incorporated into PE via the Kennedy pathway, allowing CuAAC‐based visualization of PE and affinity capture of PE‐conjugated LC3, ubiquitin, and GPI‐anchored proteins.
Cho YT, Jao CY, Xia Z, White-Mathieu BM, Salic A, Baskin JM.   +5 more
europepmc   +3 more sources