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Structure of GABARAP in two conformations: implications for GABA(A) receptor localization and tubulin binding.

Neuron | Jan 3, 2002

http://www.ncbi.nlm.nih.gov/pubmed/11779480

GABARAP recognizes and binds the gamma2 subunit of the GABA(A) receptor, interacts with microtubules and the N-ethyl maleimide sensitive factor, and is proposed to function in GABA(A) receptor trafficking and postsynaptic localization. We have determined the crystal structure of human GABARAP at 1.6 A resolution. The structure comprises an N-terminal helical subdomain and a ubiquitin-like C-terminal domain. Structure-based mutational analysis demonstrates that the N-terminal subdomain is responsible for tubulin binding while the C-terminal domain contains the binding site for the GABA(A). A second GABARAP crystal form was determined at 1.9 A resolution and documents that GABARAP can self-associate in a head-to-tail manner. The structural details of this oligomerization reveal how GABARAP can both promote tubulin polymerization and facilitate GABA(A) receptor clustering.

Pubmed ID: 11779480 RIS Download

Mesh terms: Adaptor Proteins, Signal Transducing | Animals | Binding Sites | Humans | Microtubule-Associated Proteins | Microtubules | Molecular Sequence Data | Neural Inhibition | Polymers | Protein Structure, Tertiary | Protein Transport | Receptors, GABA-A | Sequence Homology, Amino Acid | Synaptic Membranes | Synaptic Transmission | Tubulin

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Mouse Genome Informatics (Data, Gene Annotation)

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