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• W1963574116 endingPage "e26283" @default.
• W1963574116 startingPage "e26283" @default.
• W1963574116 abstract "Calcium ion (Ca2+) concentration plays a key role in cell signaling in eukaryotic cells. At the cellular level, Ca2+ directly participates in such diverse cellular events as adhesion and migration, differentiation, contraction, secretion, synaptic transmission, fertilization, and cell death. As a consequence of these diverse actions, the cytosolic concentration of free Ca2+ is tightly regulated by the coordinated activity of Ca2+ channels, Ca2+ pumps, and Ca2+-binding proteins. Although many of these regulators have been studied in depth, other proteins have been described recently, and naturally far less is known about their contribution to cell physiology. Within this last group of proteins, STIM1 has emerged as a major contributor to Ca2+ signaling by means of its activity as Ca2+ channel regulator. STIM1 is a protein resident mainly, but not exclusively, in the endoplasmic reticulum (ER), and activates a set of plasma membrane Ca2+ channels termed store-operated calcium channels (SOCs) when the concentration of free Ca2+ within the ER drops transiently as a result of Ca2+ release from this compartment. Knowledge regarding the molecular architecture of STIM1 has grown considerably during the last years, and several structural domains within STIM1 have been reported to be required for the specific molecular interactions with other important players in Ca2+ signaling, such as Ca2+ channels and microtubules. Within the modulators of STIM1, phosphorylation has been shown to both activate and inactivate STIM1-dependent Ca2+ entry depending on the cell type, cell cycle phase, and the specific residue that becomes modified. Here we shall review current knowledge regarding the modulation of STIM1 by phosphorylation." @default.
• W1963574116 created "2016-06-24" @default.
• W1963574116 creator A5016076344 @default.
• W1963574116 creator A5036262144 @default.
• W1963574116 date "2013-11-09" @default.
• W1963574116 modified "2023-10-16" @default.
• W1963574116 title "The regulation of STIM1 by phosphorylation" @default.
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• W1963574116 doi "https://doi.org/10.4161/cib.26283" @default.
• W1963574116 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3914909" @default.
• W1963574116 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24505502" @default.
• W1963574116 hasPublicationYear "2013" @default.
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