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Alternative splice variants of hTrp4 differentially interact with the C-terminal portion of the inositol 1,4,5-trisphosphate receptors.
- Source :
-
FEBS letters [FEBS Lett] 2001 Jan 05; Vol. 487 (3), pp. 377-83. - Publication Year :
- 2001
-
Abstract
- The molecular basis of capacitative (or store-operated) Ca2+ entry is still subject to debate. The transient receptor potential proteins have been hypothesized to be structural components of store-operated Ca2+ channels and recent evidence suggests that Trp3 and its closely related homolog Trp6 are gated by the N-terminal region of the inositol 1,4,5-triphosphate receptors (InsP3R). In this study, we report the existence of two isoforms of the human Trp4 protein, referred to as alpha-hTrp4 and beta-hTrp4. The shorter variant beta-hTrp4 is generated through alternative splicing and lacks the C-terminal amino acids G785-S868. Using a yeast two-hybrid assay and glutathione-S-transferase-pulldown experiments, we found that the C-terminus of alpha-hTrp4, but not of beta-hTrp4, associates in vitro with the C-terminal domain of the InsP(3) receptors type 1, 2 and 3. Thus, we describe a novel interaction between Trp proteins and InsP3R and we provide evidence suggesting that the formation of hTrp4-InsP3R complexes may be regulated by alternative splicing.
- Subjects :
- Alternative Splicing
Amino Acid Sequence
Animals
Base Sequence
Binding Sites
Calcium Channels classification
DNA Primers genetics
Humans
In Vitro Techniques
Inositol 1,4,5-Trisphosphate Receptors
Molecular Sequence Data
Protein Isoforms chemistry
Protein Isoforms genetics
Protein Isoforms metabolism
RNA, Messenger genetics
RNA, Messenger metabolism
Rats
Receptors, Cytoplasmic and Nuclear classification
Receptors, Cytoplasmic and Nuclear genetics
Sequence Homology, Amino Acid
TRPC Cation Channels
Tissue Distribution
Two-Hybrid System Techniques
Calcium Channels chemistry
Calcium Channels genetics
Calcium Channels metabolism
Receptors, Cytoplasmic and Nuclear chemistry
Receptors, Cytoplasmic and Nuclear metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 487
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 11163362
- Full Text :
- https://doi.org/10.1016/s0014-5793(00)02362-0