Toward IP3 Biosensors

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Science  08 Feb 2002:
Vol. 295, Issue 5557, pp. 931
DOI: 10.1126/science.295.5557.931d

Many cellular functions are regulated by the second messenger D-myo-inositol-1,4,5-trisphosphate (IP3), which helps regulate intracellular Ca2+ concentrations. The concentration of small ionic species such as Ca2+ can be mapped in cells by using fluorescent sensors, but IP3 must be assayed with ex situ methods such as high-performance liquid chromatography.

Morii et al. report on progress toward an IP3 biosensor based on binding by the pleckstrin homology (PH) domain of rat phospholipase C d (PLCd). They mutated three amino acids (Arg56, Val58, and Asn106) to cysteine and then labeled these sites with one of four thiol-reactive dyes. Several of the labeled PH domains showed large changes in fluorescence in response to micromolar solutions of IP3. The labeled PH domains also showed greater selectivity for IP3 as compared with other inositols. — PDS

J. Am. Chem. Soc. 10.1021/ja016824d.

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