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The transient receptor potential channels TRPP2 and TRPC1 form a heterotetramer with a 2:2 stoichiometry and an alternating subunit arrangement.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2009 Dec 18; Vol. 284 (51), pp. 35507-13. - Publication Year :
- 2009
-
Abstract
- There is functional evidence that polycystin-2 (TRPP2) interacts with other members of the transient receptor potential family, including TRPC1 and TRPV4. Here we have used atomic force microscopy to study the structure of the TRPP2 homomer and the interaction between TRPP2 and TRPC1. The molecular volumes of both Myc-tagged TRPP2 and V5-tagged TRPC1 isolated from singly transfected tsA 201 cells indicated that they assembled as homotetramers. The molecular volume of the protein isolated from cells expressing both TRPP2 and TRPC1 was intermediate between the volumes of the two homomers, suggesting that a heteromer was being formed. The distribution of angles between pairs of anti-Myc antibodies bound to TRPP2 particles had a large peak close to 90 degrees and a smaller peak close to 180 degrees , consistent with the assembly of TRPP2 as a homotetramer. In contrast, the corresponding angle distributions for decoration of the TRPP2-TRPC1 heteromer by either anti-Myc or anti-V5 antibodies had predominant peaks close to 180 degrees . This decoration pattern indicates a TRPP2:TRPC1 subunit stoichiometry of 2:2 and an alternating subunit arrangement.
- Subjects :
- Cell Line
Humans
Microscopy, Atomic Force methods
Multiprotein Complexes genetics
Multiprotein Complexes metabolism
Multiprotein Complexes ultrastructure
Protein Structure, Quaternary physiology
TRPC Cation Channels genetics
TRPC Cation Channels metabolism
TRPP Cation Channels genetics
TRPP Cation Channels metabolism
TRPV Cation Channels chemistry
TRPV Cation Channels genetics
TRPV Cation Channels metabolism
Multiprotein Complexes chemistry
TRPC Cation Channels chemistry
TRPP Cation Channels chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1083-351X
- Volume :
- 284
- Issue :
- 51
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 19850920
- Full Text :
- https://doi.org/10.1074/jbc.M109.060228