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NAADP mobilizes calcium from acidic organelles through two-pore channels

Zhu, Michael X ; Calcraft, Peter J ; Ruas, Margarida ; Pan, Zui ; Cheng, Xiaotong ; Arredouani, Abdelilah ; Hao, Xuemei ; Tang, Jisen ; Rietdorf, Katja ; Teboul, Lydia ; Chuang, Kai-Ting ; Lin, Peihui ; Xiao, Rui ; Wang, Chunbo ; Zhu, Yingmin ; Lin, Yakang ; Wyatt, Christopher N ; Parrington, John ; Ma, Jianjie ; Evans, A. Mark ; Galione, Antony

Nature, 2009-05, Vol.459 (7246), p.596-600 [Periódico revisado por pares]

London: Nature Publishing Group

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NAADP mobilizes calcium from acidic organelles through two-pore channels
Autor: Zhu, Michael X ; Calcraft, Peter J ; Ruas, Margarida ; Pan, Zui ; Cheng, Xiaotong ; Arredouani, Abdelilah ; Hao, Xuemei ; Tang, Jisen ; Rietdorf, Katja ; Teboul, Lydia ; Chuang, Kai-Ting ; Lin, Peihui ; Xiao, Rui ; Wang, Chunbo ; Zhu, Yingmin ; Lin, Yakang ; Wyatt, Christopher N ; Parrington, John ; Ma, Jianjie ; Evans, A. Mark ; Galione, Antony
Assuntos: Animals ; Biological and medical sciences ; Calcium ; Calcium - metabolism ; Calcium Channels - genetics ; Calcium Channels - metabolism ; Calcium Signaling - drug effects ; Calcium, Dietary ; Cell Line ; Cell membranes. Ionic channels. Membrane pores ; Cell organelles ; Cell structures and functions ; Cells ; Cellular control mechanisms ; Chemical properties ; Chickens ; Fundamental and applied biological sciences. Psychology ; Humans ; Hydrogen-Ion Concentration ; Insulin-Secreting Cells - drug effects ; Insulin-Secreting Cells - metabolism ; Ion channels ; Mice ; Mice, Knockout ; Molecular and cellular biology ; Molecular biology ; Molecular Sequence Data ; NADP (Coenzyme) ; NADP - analogs & derivatives ; NADP - metabolism ; NADP - pharmacology ; Organelles - drug effects ; Organelles - metabolism ; Properties ; Protein Binding
É parte de: Nature, 2009-05, Vol.459 (7246), p.596-600
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Equal contributing authors
Descrição: Ca2+ mobilization from intracellular stores represents an important cell signalling process that is regulated, in mammalian cells, by inositol-1,4,5-trisphosphate (InsP3), cyclic ADP ribose and nicotinic acid adenine dinucleotide phosphate (NAADP). InsP3 and cyclic ADP ribose cause the release of Ca2+ from sarcoplasmic/endoplasmic reticulum stores by the activation of InsP3 and ryanodine receptors (InsP3Rs and RyRs). In contrast, the nature of the intracellular stores targeted by NAADP and the molecular identity of the NAADP receptors remain controversial, although evidence indicates that NAADP mobilizes Ca2+ from lysosome-related acidic compartments. Here we show that two-pore channels (TPCs) comprise a family of NAADP receptors, with human TPC1 (also known as TPCN1) and chicken TPC3 (TPCN3) being expressed on endosomal membranes, and human TPC2 (TPCN2) on lysosomal membranes when expressed in HEK293 cells. Membranes enriched with TPC2 show high affinity NAADP binding, and TPC2 underpins NAADP-induced Ca2+ release from lysosome-related stores that is subsequently amplified by Ca2+-induced Ca2+ release by InsP3Rs. Responses to NAADP were abolished by disrupting the lysosomal proton gradient and by ablating TPC2 expression, but were only attenuated by depleting endoplasmic reticulum Ca2+ stores or by blocking InsP3Rs. Thus, TPCs form NAADP receptors that release Ca2+ from acidic organelles, which can trigger further Ca2+ signals via sarcoplasmic/endoplasmic reticulum. TPCs therefore provide new insights into the regulation and organization of Ca2+ signals in animal cells, and will advance our understanding of the physiological role of NAADP.
Editor: London: Nature Publishing Group
Idioma: Inglês

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NAADP mobilizes calcium from acidic organelles through two-pore channels

London: Nature Publishing Group

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