Structure-function analysis of TRPV channels

Niemeyer, Barbara A.

doi:10.1007/s00210-005-1053-7

Cited by 39 publications

(21 citation statements)

References 110 publications

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“…Indeed TRPV5 and TRPV6 have been shown to assemble through an interaction between their ankyrin repeat domains. These two channels, which are involved in epithelial Ca 2ϩ uptake (25), contain six ankyrin repeats in the N terminus (21), whereas TRPCs contain only four ankyrin repeats (26). For TRPV6, two interactions have been described: a self-interaction of the third ankyrin repeat and a self-interaction of the fifth ankyrin repeat (27).…”

Section: Discussionmentioning

confidence: 99%

Identification of Two Domains Involved in the Assembly of Transient Receptor Potential Canonical Channels

Lepage

Lussier

Barajas-Martínez

et al. 2006

Journal of Biological Chemistry

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Transient receptor potential canonical (TRPC) channels are associated with calcium entry activity in nonexcitable cells. TRPCs can form homo-or heterotetrameric channels, in which case they can assemble together within a subfamily groups. TRPC1, 4, and 5 represent one group, and TRPC3, 6, and 7 represent the other. The molecular determinants involved in promoting subunit tetramerization are not known. To identify them, we generated chimeras by swapping the different domains of TRPC4 with the same regions in TRPC6. We showed that TRPC4 coimmunoprecipitated with the chimeras containing the ankyrin repeats and coiled-coil domains of TRPC4 into TRPC6. However, chimeras containing only the ankyrin repeats or only the coiled-coil domain of TRPC4 did not coimmunoprecipitate with TRPC4. We also showed that a second domain of interaction composed of the pore region and the C-terminal tail is involved in the oligomerization of TRPC4. However, chimeras containing only the pore region or only the C-terminal tail of TRPC4 did not coimmunoprecipitate with TRPC4. Furthermore, we showed that the N terminus of TRPC6 coimmunoprecipitated with the C terminus of TRPC6. Overexpression in HEK293T cells of chimeras that contained an N terminus and a C terminus from different subfamily groups increased intracellular calcium entry subsequent to stimulation of G q proteincoupled receptors. These results suggest that two types of interactions are involved in the assembly of the four subunits of the TRPC channel. The first interaction occurs between the N termini and involves two regions. The second interaction occurs between the N terminus and the C terminus and does not appear to be necessary for the activity of TRPCs.Calcium signaling is involved in many cellular functions, including cell growth, differentiation, contraction, and secretion. The elevation of [Ca 2ϩ ] i occurs via two distinct phases upon activation of a G q protein-coupled receptor or a tyrosine kinase receptor. The first phase is mediated through the activation of phospholipase C, which catalyzes the production of inositol 1,4,5-trisphosphate, which in turn mobilizes Ca 2ϩ from the endoplasmic reticulum. The second phase of [Ca 2ϩ ] i elevation involves Ca 2ϩ entry from the extracellular milieu that maintains the [Ca 2ϩ ] i higher than the basal level (1, 2). The transient receptor potential canonical (TRPC) 3 protein family is involved in calcium entry and is composed of seven members (TRPC1 to TRPC7) that are calcium-permeable cation channels (3, 4). Based on sequence similarity, TRPCs can be further subdivided into four groups. Groups 1 and 2 contain exclusively the isoforms TRPC1 and TRPC2, respectively. Group 3 includes TRPC3, TRPC6, and TRPC7, whereas group 4 includes TRPC4 and TRPC5. Group 4 TRPCs are most closely related to group 1. TRPCs consist of a transmembrane domain composed of six segments with a putative pore between the fifth and the sixth transmembrane segments. The transmembrane domain is flanked with cytoplasmic N and C termini (5). TRPCs posse...

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Section: Discussionmentioning

confidence: 99%

Identification of Two Domains Involved in the Assembly of Transient Receptor Potential Canonical Channels

Lepage

Lussier

Barajas-Martínez

et al. 2006

Journal of Biological Chemistry

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“…The TRPV cation channel family shows homeostatic and regulatory functions (calcium influx, apoptosis, and cell proliferation). In addition, recent data indicate that changes in their expression contribute to malignant growth and progression [11,12] and a role for TRPV6 and TRPV1 in the progression of prostate and bladder cancer and gliomas was reported [13][14][15]. At present, no data concerning the TRPV2 channel expression in normal and tumour human bladder tissues are available, and it is still unknown whether changes in TRPV2 expression could be associated with the disease stage in UC.…”

Section: Introductionmentioning

confidence: 99%

Transient Receptor Potential Vanilloid Type 2 (TRPV2) Expression in Normal Urothelium and in Urothelial Carcinoma of Human Bladder: Correlation with the Pathologic Stage

et al. 2008

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“…The rest of the protein including intracellular N-and C-terminal sequences forms the large cytoplasmic region and comprises Ϸ70% of the protein mass. TRPV1 functions as a nonselective tetrameric cation channel with a high permeability to calcium (permeability sequence Ca 2ϩ Ͼ Mg ϩ2 Ͼ Na ϩ Ϸ K ϩ Ϸ Cs ϩ ) (15,16).…”

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confidence: 99%

Structure of TRPV1 channel revealed by electron cryomicroscopy

Moiseenkova-Bell

Stanciu

Serysheva

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

190

176

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The transient receptor potential (TRP) family of ion channels participate in many signaling pathways. TRPV1 functions as a molecular integrator of noxious stimuli, including heat, low pH, and chemical ligands. Here, we report the 3D structure of fulllength rat TRPV1 channel expressed in the yeast Saccharomyces cerevisiae and purified by immunoaffinity chromatography. We demonstrate that the recombinant purified TRPV1 channel retains its structural and functional integrity and is suitable for structural analysis. The 19-Å structure of TRPV1 determined by using singleparticle electron cryomicroscopy exhibits fourfold symmetry and comprises two distinct regions: a large open basket-like domain, likely corresponding to the cytoplasmic N-and C-terminal portions, and a more compact domain, corresponding to the transmembrane portion. The assignment of transmembrane and cytoplasmic regions was supported by fitting crystal structures of the structurally homologous Kv1.2 channel and isolated TRPV1 ankyrin repeats into the TRPV1 structure.cryoelectron microscopy ͉ ion channels ͉ TRP channels

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Structure-function analysis of TRPV channels

Cited by 39 publications

References 110 publications

Identification of Two Domains Involved in the Assembly of Transient Receptor Potential Canonical Channels

Identification of Two Domains Involved in the Assembly of Transient Receptor Potential Canonical Channels

Transient Receptor Potential Vanilloid Type 2 (TRPV2) Expression in Normal Urothelium and in Urothelial Carcinoma of Human Bladder: Correlation with the Pathologic Stage

Structure of TRPV1 channel revealed by electron cryomicroscopy

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