Evolutionary origins of STIM1 and STIM2 within ancient Ca2+ signaling systems

Sean Collins, Tobias Meyer

Research output: Contribution to journalReview article

64 Citations (Scopus)

Abstract

Human stromal interaction molecule (STIM) proteins are parts of elaborate eukaryotic Ca2+ signaling systems that include numerous plasma membrane (PM), endoplasmic reticulum (ER), and mitochondrial Ca2+ transporters, channels and regulators. STIM2 and STIM1 function as Ca2+ sensors with different sensitivities for ER Ca2+. They translocate to ER-PM junctions and open PM Orai Ca2+ influx channels when receptor-mediated Ca2+ release lowers ER Ca2+ levels. The resulting increase in cytosolic Ca2+ leads to the activation of numerous Ca2+ effector proteins that in turn regulate differentiation, cell contraction, secretion and other cell functions. In this review, we use an evolutionary perspective to survey molecular activation mechanisms in the Ca2+ signaling system, with a particular focus on regulatory motifs and functions of the two STIM proteins. We discuss the presence and absence of STIM genes in different species, the order of appearance of STIM versus Orai, and the evolutionary addition of new signaling domains to STIM proteins.

Original languageEnglish (US)
Pages (from-to)202-211
Number of pages10
JournalTrends in Cell Biology
Volume21
Issue number4
DOIs
StatePublished - Apr 1 2011
Externally publishedYes

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Endoplasmic Reticulum
Cell Membrane
Proteins
Cell Differentiation
Stromal Interaction Molecules
Genes

ASJC Scopus subject areas

  • Cell Biology

Cite this

Evolutionary origins of STIM1 and STIM2 within ancient Ca2+ signaling systems. / Collins, Sean; Meyer, Tobias.

In: Trends in Cell Biology, Vol. 21, No. 4, 01.04.2011, p. 202-211.

Research output: Contribution to journalReview article

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