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. 2011 Dec 19;2(12):990–996. doi: 10.1007/s13238-011-1116-0

ERp44 C160S/C212S mutants regulate IP3R1 channel activity

Congyan Pan 1, Ji Zheng 2, Yanyun Wu 1, Yingxiao Chen 1, Likun Wang 1, Zhansong Zhou 2, Wenxuan Yin 1,✉, Guangju Ji 1,✉
PMCID: PMC4875245  PMID: 22183808

Abstract

Previous studies have indicated that ERp44 inhibits inositol 1,4,5-trisphosphate (IP3)-induced Ca2+ release (IICR) via IP3R1, but the mechanism remains largely unexplored. Using extracellular ATP to induce intracellular calcium transient as an IICR model, Ca2+ image, pull down assay, and Western blotting experiments were carried out in the present study. We found that extracellular ATP induced calcium transient via IP3Rs (IICR) and the IICR were markedly decreased in ERp44 overexpressed Hela cells. The inhibitory effect of C160S/C212S but not C29S/T396A/ΔT(331–377) mutants of ERp44 on IICR were significantly decreased compared with ERp44. However, the binding capacity of ERp44 to L3V domain of IP3R1 (1L3V) was enhanced by ERp44 C160S/C212S mutation. Taken together, these results suggest that the mutants of ERp44, C160/C212, can more tightly bind to IP3R1 but exhibit a weak inhibition of IP3R1 channel activity in Hela cells.

Keywords: ERp44; mutants; ATP; inositol 1,4,5-trisphosphate (IP3) receptors; calcium transient

Footnotes

These authors contributed equally to the work.

Contributor Information

Wenxuan Yin, Email: Yinw@moon.ibp.ac.cn.

Guangju Ji, Email: Gj28@ibp.ac.cn.

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