GABARAP and GABA(A) receptor clustering.
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
WD
Department of Physiology, University of Sydney, NSW 2006, Australia.
Froehner
Stanley C
SC
D048868:Adaptor Proteins, Signal Transducing; D000818:Animals; D051017:Apoptosis Regulatory Proteins; D002352:Carrier Proteins / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D051379:Mice; D008869:Microtubule-Associated Proteins / Q000737:chemistry*; D008870:Microtubules / Q000378:metabolism*; D009433:Neural Inhibition / Q000502:physiology*; D017434:Protein Structure, Tertiary / Q000502:physiology; D021381:Protein Transport / Q000502:physiology*; D011963:Receptors, GABA-A / Q000378:metabolism*; D009435:Synaptic Transmission / Q000502:physiology*
D048868:Adaptor Proteins, Signal Transducing; D051017:Apoptosis Regulatory Proteins; D002352:Carrier Proteins; C116741:GABARAP protein, human; D008565:Membrane Proteins; D008869:Microtubule-Associated Proteins; D011963:Receptors, GABA-A; C073441:gephyrin