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The TRP Channels, a Remarkably Functional Family
TRP cation channels display an extraordinary assortment of selectivities and activation mechanisms, some of which represent previously unrecognized modes for regulating ion channels. Moreover, the
Functional interaction between InsP3 receptors and store-operated Htrp3 channels
It is shown that Htrp3 channels stably expressed in HEK293 cells are in a tight functional interaction with the InsP3 receptors, providing evidence for the coupling hypothesis, in which InsP 3 receptors activated by InsP2 interact with SOC and regulate Icrac.
Nomenclature of Voltage-Gated Calcium Channels
A new nomen-ties of the channel complex, the pharmacological and clature of voltage-gated Ca 2ϩ channels, which electrophysiological diversity of Ca 2 ϩ channels arises is more systematic and mimics the well-defined K ϩ primarily from the existence of multiple forms of ␣ 1 sub-channel nomenclature.
Requirement of the inositol trisphosphate receptor for activation of store-operated Ca2+ channels.
It is concluded that insP3Rs mediate both SOC and TRP channel opening and that the InsP3R is essential for maintaining coupling between store emptying and physiological activation of SOCs.
Increased Vascular Smooth Muscle Contractility in TRPC6−/− Mice
It is implied that constitutively active TRPC3-type channels, which are up-regulated in TRPC6-deficient smooth muscle cells, are not able to functionally replace TRPC 6, which has distinct nonredundant roles in the control of vascular smooth muscle tone.
Identification of Common Binding Sites for Calmodulin and Inositol 1,4,5-Trisphosphate Receptors on the Carboxyl Termini of Trp Channels*
The data support the view that both CaM and IP3Rs play important roles in controlling the gating of Trp-based channels, however, the sensitivity and responses toCaM andIP3Rs differ for each Trp.
Receptor-activated Ca2+ Influx via Human Trp3 Stably Expressed in Human Embryonic Kidney (HEK)293 Cells
  • Xi Zhu, Meisheng Jiang, L. Birnbaumer
  • Biology, Medicine
    The Journal of Biological Chemistry
  • 2 January 1998
It is proposed that expression of hTrp3 in these cells forms a non-selective cation channel that opens after the activation of phospholipase C but not after store depletion, which may form heteromultimeric channels with endogenous proteins that are sensitive to store depletion.
A unified nomenclature for the superfamily of TRP cation channels.
The current effort to unify the TRP nomenclature focuses on three subfamilies that bear significant similarities to the founding member of this superfamily, Drosophila TRP, and which include highly related members in worms, flies, mice, and humans.
Direct interaction of Gβγ with a C-terminal Gβγ-binding domain of the Ca2+ channel α1 subunit is responsible for channel inhibition by G protein-coupled receptors
The results define the molecular mechanism by which presynaptic G protein-coupled receptors inhibit neurotransmission and do not support proposals that Gβγ inhibits α1 function by interacting with the site located in the loop I–II linker.
On the molecular basis and regulation of cellular capacitative calcium entry: roles for Trp proteins.
The hypothesis that CCE channels are formed of subunits encoded in genes related to the Drosophila trp gene was tested and provided a firm connection between CCE and mammalian Trps.