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

Temple University

Research output: Contribution to journal › Review article › peer-review

589 Scopus citations

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.

Original language	English
Pages (from-to)	549-565
Number of pages	17
Journal	Nature Reviews Molecular Cell Biology
Volume	13
Issue number	9
DOIs	https://doi.org/10.1038/nrm3414
State	Published - Sep 2012

Keywords

Animals
Calcium Signaling
Calcium/metabolism
Cell Adhesion Molecules/metabolism
Cell Membrane/metabolism
Endoplasmic Reticulum/metabolism
Humans
Intercellular Junctions/metabolism
Membrane Proteins/metabolism
Models, Biological
Neoplasm Proteins/metabolism
Stromal Interaction Molecule 1
Stromal Interaction Molecule 2

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10.1038/nrm3414

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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.",

keywords = "Animals, Calcium Signaling, Calcium/metabolism, Cell Adhesion Molecules/metabolism, Cell Membrane/metabolism, Endoplasmic Reticulum/metabolism, Humans, Intercellular Junctions/metabolism, Membrane Proteins/metabolism, Models, Biological, Neoplasm Proteins/metabolism, Stromal Interaction Molecule 1, Stromal Interaction Molecule 2",

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

year = "2012",

month = sep,

doi = "10.1038/nrm3414",

language = "English",

volume = "13",

pages = "549--565",

journal = "Nature Reviews Molecular Cell Biology",

issn = "1471-0072",

publisher = "Nature Research",

number = "9",

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TY - JOUR

T1 - STIM proteins

T2 - Dynamic calcium signal transducers

AU - Soboloff, Jonathan

AU - Rothberg, Brad S.

AU - Madesh, Muniswamy

AU - Gill, Donald L.

PY - 2012/9

Y1 - 2012/9

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.

KW - Animals

KW - Calcium Signaling

KW - Calcium/metabolism

KW - Cell Adhesion Molecules/metabolism

KW - Cell Membrane/metabolism

KW - Endoplasmic Reticulum/metabolism

KW - Humans

KW - Intercellular Junctions/metabolism

KW - Membrane Proteins/metabolism

KW - Models, Biological

KW - Neoplasm Proteins/metabolism

KW - Stromal Interaction Molecule 1

KW - Stromal Interaction Molecule 2

UR - https://www.scopus.com/pages/publications/84865414921

U2 - 10.1038/nrm3414

DO - 10.1038/nrm3414

M3 - Review article

C2 - 22914293

SN - 1471-0072

VL - 13

SP - 549

EP - 565

JO - Nature Reviews Molecular Cell Biology

JF - Nature Reviews Molecular Cell Biology

IS - 9

ER -

STIM proteins: Dynamic calcium signal transducers

Abstract

Keywords

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