Premium
Alternative splice variants of hTrp4 differentially interact with the C‐terminal portion of the inositol 1,4,5‐trisphosphate receptors
Author(s) -
Mery Laurence,
Magnino Fabrice,
Schmidt Karin,
Krause Karl-Heinz,
Dufour Jean-François
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02362-0
Subject(s) - alternative splicing , receptor , gene isoform , splice , inositol , rna splicing , c terminus , biochemistry , biology , microbiology and biotechnology , amino acid , chemistry , gene , rna
The molecular basis of capacitative (or store‐operated) Ca 2+ entry is still subject to debate. The transient receptor potential proteins have been hypothesized to be structural components of store‐operated Ca 2+ 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 (InsP 3 R). In this study, we report the existence of two isoforms of the human Trp4 protein, referred to as α‐hTrp4 and β‐hTrp4. The shorter variant β‐hTrp4 is generated through alternative splicing and lacks the C‐terminal amino acids G 785 –S 868 . Using a yeast two‐hybrid assay and glutathione‐ S ‐transferase‐pulldown experiments, we found that the C‐terminus of α‐hTrp4, but not of β‐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 InsP 3 R and we provide evidence suggesting that the formation of hTrp4–InsP 3 R complexes may be regulated by alternative splicing.