FMP Publications

Our publications are recorded in a searchable database since 2010, updates will be added regularly.

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References
Cellular strategies to cope with protein aggregation
Scior, A., Jünemann, K.; Kirstein, J.
In VanOostenHawle, P., editor, Volume 60 of Essays in Biochemistry
page 153-161.
Publisher: Portland Press Ltd, London
(2016)
OA-Link

Tags: Proteostasis in Aging and Disease (Kirstein)

Abstract: Nature has evolved several mechanisms to detoxify intracellular protein aggregates that arise upon proteotoxic challenges. These include the controlled deposition of misfolded proteins at distinct cellular sites, the protein disaggregation and refolding by molecular chaperones and/or degradation of misfolded and aggregated protein species by cellular clearance pathways. In this article, we discuss cellular the strategies of prokaroytes and eukaryotes to control protein aggregation.

Structural rearrangement of the intracellular domains during AMPA receptor activation
Zachariassen(*), L. G., Katchan, L., Jensen(*), A. G., Pickering(*), D. S., Plested, A. J.; Kristensen(*), A. S.
Proc Natl Acad Sci U S A, 113:E3950-3959
(2016)

Tags: Molecular Neuroscience and Biophysics (Plested)

Abstract: alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs) are ligand-gated ion channels that mediate the majority of fast excitatory neurotransmission in the central nervous system. Despite recent advances in structural studies of AMPARs, information about the specific conformational changes that underlie receptor function is lacking. Here, we used single and dual insertion of GFP variants at various positions in AMPAR subunits to enable measurements of conformational changes using fluorescence resonance energy transfer (FRET) in live cells. We produced dual CFP/YFP-tagged GluA2 subunit constructs that had normal activity and displayed intrareceptor FRET. We used fluorescence lifetime imaging microscopy (FLIM) in live HEK293 cells to determine distinct steady-state FRET efficiencies in the presence of different ligands, suggesting a dynamic picture of the resting state. Patch-clamp fluorometry of the double- and single-insert constructs showed that both the intracellular C-terminal domain (CTD) and the loop region between the M1 and M2 helices move during activation and the CTD is detached from the membrane. Our time-resolved measurements revealed unexpectedly complex fluorescence changes within these intracellular domains, providing clues as to how posttranslational modifications and receptor function interact.

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Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP)
Campus Berlin-Buch
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