Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Schindl, R; Frischauf, I; Kahr, H; Fritsch, R; Krenn, M; Derndl, A; Vales, E; Muik, M; Derler, I; Groschner, K; Romanin, C.
The first ankyrin-like repeat is the minimum indispensable key structure for functional assembly of homo- and heteromeric TRPC4/TRPC5 channels.
Cell Calcium. 2008; 43(3): 260-269.
Doi: 10.1016/j.ceca.2007.05.015
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- Führende Autor*innen der Med Uni Graz
- Schindl Rainer
- Co-Autor*innen der Med Uni Graz
- Groschner Klaus
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- Abstract:
- The closely related TRPC4 and TRPC5 proteins, members of the canonical transient receptor potential (TRPC) family, assemble into either homo- or heterotetrameric, non-selective cation-channels. To elucidate domains that mediate channel complex formation, we evaluated dominant negative effects of N- or C-terminal TRPC4/5 fragments on respective currents of full-length proteins overexpressed in HEK293 cells with whole-cell electrophysiology. Confocal Förster Resonance Energy Transfer (FRET) measurements enabled to probe the interaction potential of these CFP/YFP-labelled fragments in vivo. Only N-terminal fragments that included the first ankyrin-like repeat potently down-regulated TRPC4/TRPC5 currents, while fragments including either the second ankyrin-like repeat and the coiled-coil domain or the C-terminus remained ineffective. Total internal reflection fluorescence (TIRF) microscopy data suggested that the dominant negative N-terminal fragments led to a predominantly intracellular localisation of coexpressed TRPC5 proteins. FRET measurements clearly revealed that only fragments including the first ankyrin-like repeat were able to multimerise. Moreover a TRPC5 mutant that lacked the first ankyrin-like repeat was unable to homo-multimerise, failed to interact with wild-type TRPC5 and resulted in non-functional channels.
- Find related publications in this database (using NLM MeSH Indexing)
- Amino Acid Sequence -
- Animals -
- Ankyrin Repeat -
- Cell Line -
- Genes, Dominant -
- Humans -
- Ion Channel Gating -
- Mice -
- Molecular Sequence Data -
- Mutant Proteins -
- Peptide Fragments - chemistry
- Peptide Fragments - metabolism
- Protein Binding -
- Protein Structure, Quaternary -
- Structure-Activity Relationship -
- TRPC Cation Channels - chemistry
- TRPC Cation Channels - metabolism
- Find related publications in this database (Keywords)
- TRPC
- transient receptor potential
- channel
- assembly
- ankyrin