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Structure and function of calcium signalling pathways

 Current vacancies for 2 postdocs

 

Professor Colin W. Taylor

E-Mail: cwt1000@cam.ac.uk

Tel: +44 1223 334058/334062

 

Colin Taylor’s lab typically includes about twelve staff (with almost as many nationalities), including postdocs, a lab manager, PhD students and visitors. Our well-equipped lab is housed in a modern department situated close to the historic city centre and a short walk from the railway station. Our work is concerned with understanding how intracellular calcium signals are generated and decoded. Several groups within the department share interests in cell signalling, allowing us to share resources and weekly lab meetings. We also enjoy inter-disciplinary collaborations with other labs in the UK and abroad.

We welcome informal enquires from students and postdocs wanting to join the lab.

 

 

Investigator biography

Colin read Natural Sciences at Gonville and Caius College, Cambridge and then completed a PhD in insect physiology with Mike Berridge. He completed postdoctoral work with Jim Putney in the USA, before returning to Cambridge as a research fellow of St John's College and a Royal Society Locke Research Fellow. He was appointed to a lectureship in pharmacology soon afterwards, and then to a Lister Institute Research Fellowship. He was appointed Professor in Cellular Pharmacology in 2001. Colin has served on various editorial boards, and committees of funding agencies and societies, including chairing the board of Gordon Research Conferences. He is a member of Academia Europaea, a Fellow of the Academy of Medical Sciences, and a Wellcome Trust Senior Investigator. His lab is interested in calcium signalling.

Lab members

Research summary

All cells must sense their surroundings and communicate with each other. Receptors in the plasma membrane are the antennae that detect extracellular signals, and they communicate with the cell interior via intracellular messengers. Calcium ions (Ca2+), the simplest of these intracellular messengers, are used to regulate almost every cellular behaviour from fertilization to cell death. Most messengers are synthesized and degraded on-demand, but calcium is an element and so its concentration can only be regulated by moving it into and out of the cytosol across membranes. Most receptors that evoke Ca2+ signals do so by stimulating Ca2+-permeable ion channels to open, allowing Ca2+ to flow rapidly down its concentration gradient into the cytosol. Our work is primarily concerned with the most important and widely expressed of these Ca2+ channels, IP3 receptors. These reside largely within the membranes of the endoplasmic reticulum and they initiate the Ca2+ signals evoked by the many receptors that stimulate formation of IP3. We are currently addressing four major areas:

  • How do binding of IP3 and Ca2+ to the IP3 receptor, which is 5000- times larger than IP3 cause the channel to open?
  • How are signalling pathways organized to allow delivery of IP3 and other messengers to IP3 receptors?
  • How does the mobility of intracellular organelles and proteins within them contribute to the Ca2+ signals evoked by IP3?
  • How do cells decode spatially organized Ca2+ signals?

Key references

  • Srivats, S, Balasuriya, D, Pasche, M, Vistal, G, Edwardson, JM, Taylor, CW, & Murrell-Lagnado, R. (2016) Sigma 1 receptors inhibit store-operated Ca2+ entry by attenuating coupling of STIM1 to Orai1. J. Cell Biol. 213, 65-79.
  • Thurley, K, Tovey, SC, Moenke, G, Prince, VL, Meena, A, Thomas, AP, Skupin, A, Taylor, CW & Falcke, M (2014) Reliable encoding of extracellular stimuli within random sequences of Ca2+ spikes. Sci Signal. 7, ra59.
  • Saraiva, N., Prole, DL, Carrara, G, Johnson, BF, Taylor, CW, Parsons, M & Smith, GL (2013) hGAAP promotes cell adhesion and migration via the stimulation of store-operated Ca2+ entry and calpain 2. J. Cell. Biol. 202, 699-713.
  • Seo, M-D, Velamakanni, S, Ishiyama, N, Stathopulos, PB, Rossi, AM, Khan, 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.
  • 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.
  • 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.