Colin William Taylor - Selected publications#

Li, C, Seo, M-D, Enomoto, M, Rossi, AM, Rahman, T, *Taylor, CW, *Ikura, M & *Ames, JB (2013) CaBP1, a neuronal Ca2+ sensor protein, inhibits inositol trisphosphate receptors by clamping inter-subunit interactions. Proc. Natl. Acad. Sci. USA. In press. IF 9.7.
Structural and functional evidence that the neuronal Ca2+-sensor protein, CaBP1, inhibits IP3 receptors by clamping the inter-domain movements that we have suggested underlie the initial steps in IP3 receptor activation.

Seo, M-D, Velamakanni, S, Ishiyama, N, Stathopulos, PB, Rossi, AM, Kahn, SA, Dale, P, Li, C, Ames, JB, *Ikura, M & *Taylor, CW (2012) Structural and functional conservation of key domains in InsP3 and ryanodine receptors. Nature 483, 108-112. IF, 36.3. Citations: 15.
Commentary in Science Signaling (2012) 5, pe24.
The first high-resolution structures of the N-terminal of the IP3 receptor with and without IP3 bound show conformational changes evoked by IP3 binding. Docking, structural comparisons and functional analyses of chimeric receptors demonstrate that the two major families of intracellular Ca2+ channels, ryanodine and IP3 receptors, use conserved activation mechanisms.

Rossi, AM, Riley, A, Tovey, SC, Rahman, T, Dellis, O., Taylor. EJA, Veresov, V.G., Potter, BVL & Taylor CW (2009) Activation of IP3 receptors: lessons from novel partial agonists. Nature Chem. Biol. 5, 631-639. IF, 14.7. Citations: 23
Synthetic IP3 analogues are shown to bind with high-affinity to IP3 receptors but to cause less frequent channel opening than does IP3. We propose that rearrangement of relationships between the IP3-binding core and suppressor domain are the major conformational changes evoked by IP3. These are disrupted by the partial agonists.

Rahman, T-U, Skupin, A, Falcke, M & Taylor CW (2009) Clustering of IP3 receptors by IP3 retunes their regulation by IP3 and Ca2+. Nature. 458, 655-659. IF, 36.3. Citations: 67.
Featured article in Nature Signaling Gateway (March 2009); research highlight in Nature Reviews: Molecular Cell Biology 10, 238; BBSRC press release, Scientists eavesdrop on the exciting conversations within cells (http://www.bbsrc.ac.uk/media/releases/2009/090225_scientists_eavesdrop_on_cell_conversations.html).
Patch-clamp analyses of IP3 receptors in the nuclear envelope show that low concentrations of IP3 cause IP3 receptor clustering. Lone and clustered IP3 receptors respond differently to IP3 and Ca2+, and this retuning may contribute to recruitment of IP3 receptors during the elementary events observed in intact cells.

Tovey, SC, Dedos, SG, Taylor, EJA, Church, JE & Taylor CW (2008) Selective coupling of type 6 adenylyl cyclase with type 2 IP3 receptors mediates direct sensitization of IP3 receptors by cAMP. J. Cell Biol. 183, 297-311. IF, 10.3. Citations: 30.
Commentary in Science Signaling 1, ec368 (2008), and Editors' Choice in Science 322, 1026.
Parathyroid hormone, via cAMP, is shown to sensitize IP3 receptors to IP3 by a mechanism that is independent of conventional targets of cAMP. We demonstrate that cAMP is delivered at high concentrations directly to IP3 receptors within a junctional assembly of type 2 IP3 receptors and type 6 adenylyl cyclase.

Dellis, O, Dedos, SG, Tovey, SC, Rahman, U-T, Dubel, SJ & Taylor CW (2006) Ca2+ entry through plasma membrane IP3 receptors. Science 313, 229-233. IF, 31.2. Citations: 104.
Commentary in Science 313, 183-184.
Single-channel recording from B cells demonstrates that they reliably count just 1-3 functional IP3 receptors into the plasma membrane and these then mediate about half the Ca2+ entry evoked by activation of the B cell receptor; the remaining Ca2+ entry is mediated by the store-operated pathway.

Broad, L, Cannon, TR & Taylor, CW (1999) A non-capacitative pathway activated by arachidonic acid is the major Ca2+ entry in A7r5 smooth muscle cells stimulated with low concentrations of vasopressin. J. Physiol. 517, 121-134. IF, 4.9. Citations: 198.
Commentary in J. Physiol. 517, 2.
This provided some of the first evidence that receptors that stimulate phospholipase C cause activation of two distinct Ca2+ entry pathways. It challenged the notion that all Ca2+ entry is via the store-operated pathway and established the utility of Gd3+ to distinguish pathways.

Patel, S, Morris, SA, Adkins, CE, O’Beirne, G & Taylor, CW (1997) Ca2+-independent inhibition of inositol trisphosphate receptors by calmodulin: redistribution of calmodulin as a possible means of regulating Ca2+ mobilization. Proc. Natl. Acad. Sci. USA 94, 11627-11632. IF 9.7. Citations: 94
First evidence for Ca2+-independent inhibition of IP3 receptors by calmodulin. We suggested that this might set the low basal sensitivity of cerebellar IP3 receptors to IP3 and allow calmodulin redistribution to modulate the sensitivity.

Marchant, JS & Taylor, CW (1997) Cooperative activation of IP3 receptors by sequential binding of IP3 and Ca2+ safeguards against spontaneous activity. Curr. Biol. 7, 510-518. IF, 10.9. Citations: 106
Commentary in Curr. Biol. 7, R544-R547
This used novel rapid superfusion methods to demonstrate that IP3 stimulates IP3 receptors by controlling access of Ca2+ to two Ca2+-binding sites. IP3 binding causes an inhibitory site to be occluded and a stimulatory site to become exposed.

Missiaen, L, Taylor, CW & Berridge, MJ (1991) Spontaneous calcium release from inositol 1,4,5-trisphosphate-sensitive calcium stores. Nature 352, 241-244. IF, 36.3. Citations: 296
Evidence that overloading intracellular stores with Ca2+ triggers spontaneous activation of IP3 receptors, suggesting that luminal Ca2+ might be an important regulator of IP3 receptor gating.