STIM proteins: Dynamic calcium signal transducers

Jonathan Soboloff; Brad S. Rothberg; Muniswamy Madesh; Donald L. Gill

doi:10.1038/nrm3414

STIM proteins: Dynamic calcium signal transducers

Jonathan Soboloff, Brad S. Rothberg, Muniswamy Madesh, Donald L. Gill

Producción científica: Review article › revisión exhaustiva

569 Citas (Scopus)

Resumen

Stromal interaction molecule (STIM) proteins function in cells as dynamic coordinators of cellular calcium (Ca²⁺) signals. Spanning the endoplasmic reticulum (ER) membrane, they sense tiny changes in the levels of Ca²⁺ stored within the ER lumen. As ER Ca²⁺ is released to generate primary Ca²⁺ signals, STIM proteins undergo an intricate activation reaction and rapidly translocate into junctions formed between the ER and the plasma membrane. There, STIM proteins tether and activate the highly Ca²⁺-selective Orai channels to mediate finely controlled Ca ²⁺ signals and to homeostatically balance cellular Ca²⁺. Details are emerging on the remarkable organization within these STIM-induced junctional microdomains and the identification of new regulators and alternative target proteins for STIM.

Idioma original	English (US)
Páginas (desde-hasta)	549-565
Número de páginas	17
Publicación	Nature Reviews Molecular Cell Biology
Volumen	13
N.º	9
DOI	https://doi.org/10.1038/nrm3414
Estado	Published - sept 2012
Publicado de forma externa	Sí

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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title = "STIM proteins: Dynamic calcium signal transducers",

abstract = "Stromal interaction molecule (STIM) proteins function in cells as dynamic coordinators of cellular calcium (Ca2+) signals. Spanning the endoplasmic reticulum (ER) membrane, they sense tiny changes in the levels of Ca2+ stored within the ER lumen. As ER Ca2+ is released to generate primary Ca2+ signals, STIM proteins undergo an intricate activation reaction and rapidly translocate into junctions formed between the ER and the plasma membrane. There, STIM proteins tether and activate the highly Ca2+-selective Orai channels to mediate finely controlled Ca 2+ signals and to homeostatically balance cellular Ca2+. Details are emerging on the remarkable organization within these STIM-induced junctional microdomains and the identification of new regulators and alternative target proteins for STIM.",

author = "Jonathan Soboloff and Rothberg, {Brad S.} and Muniswamy Madesh and Gill, {Donald L.}",

note = "Funding Information: This work was supported by US National Institutes of Health (NIH) grants AI058173 (to D.L.G.), GM097335 (to J.S.), HL109920 (to M.M. and J.S.), HL086699 (to M.M.) and GM068523(to B.S.R.).",

year = "2012",

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AU - Soboloff, Jonathan

AU - Rothberg, Brad S.

AU - Madesh, Muniswamy

AU - Gill, Donald L.

N1 - Funding Information: This work was supported by US National Institutes of Health (NIH) grants AI058173 (to D.L.G.), GM097335 (to J.S.), HL109920 (to M.M. and J.S.), HL086699 (to M.M.) and GM068523(to B.S.R.).

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N2 - Stromal interaction molecule (STIM) proteins function in cells as dynamic coordinators of cellular calcium (Ca2+) signals. Spanning the endoplasmic reticulum (ER) membrane, they sense tiny changes in the levels of Ca2+ stored within the ER lumen. As ER Ca2+ is released to generate primary Ca2+ signals, STIM proteins undergo an intricate activation reaction and rapidly translocate into junctions formed between the ER and the plasma membrane. There, STIM proteins tether and activate the highly Ca2+-selective Orai channels to mediate finely controlled Ca 2+ signals and to homeostatically balance cellular Ca2+. Details are emerging on the remarkable organization within these STIM-induced junctional microdomains and the identification of new regulators and alternative target proteins for STIM.

AB - Stromal interaction molecule (STIM) proteins function in cells as dynamic coordinators of cellular calcium (Ca2+) signals. Spanning the endoplasmic reticulum (ER) membrane, they sense tiny changes in the levels of Ca2+ stored within the ER lumen. As ER Ca2+ is released to generate primary Ca2+ signals, STIM proteins undergo an intricate activation reaction and rapidly translocate into junctions formed between the ER and the plasma membrane. There, STIM proteins tether and activate the highly Ca2+-selective Orai channels to mediate finely controlled Ca 2+ signals and to homeostatically balance cellular Ca2+. Details are emerging on the remarkable organization within these STIM-induced junctional microdomains and the identification of new regulators and alternative target proteins for STIM.

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STIM proteins: Dynamic calcium signal transducers

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