UCL University College London Eprints
UCL Eprints collects the work of UCL researchers and makes it freely available over the web, helping the worldwide scholarly community to discover UCL research. Institutional repositories like UCL Eprints complement the traditional academic publishing and scholarly communications processes. They raise the visibility of research and help to maximise its impact. UCL researchers are encouraged to deposit a copy of each journal article, conference paper, working paper, and any other research output, in the UCL Eprints at the earliest opportunity, ensuring that their research reaches as wide an audience as possible.
Structure and trafficking of NMDA and GABAA receptors. - Stephenson, FA
The fidelity of synaptic function is dependent on the expression of the appropriate neurotransmitter receptor subtype, the targeting and trafficking of receptors to synapses as well as the regulation of the actual number of receptors at synapses. GABAA (gamma-aminobutyric acid type A) receptors and NMDA (N-methyl-D-aspartate) receptors are both examples of ligand-gated, heteromeric neurotransmitter receptors whose cell-surface expression is dynamic and tightly regulated. NMDA receptors are localized at excitatory synapses. These synapses are highly structured but dynamic, with the interplay between NMDA receptors and NMDA receptor-associated scaffolding proteins regulating the expression of functional cell-surface synaptic and extrasynaptic receptors. Based on...
GRIF-1-kinesin-1 interactions: a confocal microscopy study. - Pozo, K; Stephenson, FA
GRIF-1 [GABA(A) (gamma-aminobutyric acid(A)) receptor interacting factor-1] is a member of a coiled-coil family of proteins thought to function as adaptors in the anterograde trafficking of organelles utilizing the kinesin-1 motor proteins to synapses. To study in more detail the molecular interaction between GRIF-1 and the kinesin-1 family member KIF5C, fluorescent yellow- and fluorescent cyan-tagged GRIF-1, KIF5C, the KIF5C MD (motor domain) and the KIF5C NMD (non-motor domain) fusion proteins were generated. Each was characterized with respect to size and ability to co-associate by immunoprecipitation following expression in HEK-293 (human embryonic kidney 293) cells. Further, their distribution in transfected HEK-293...