The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
STIM1 has a plasma membrane role in the activation of store-operated Ca 2+ channels
Abstract
Receptor-induced Ca 2+ signals are key to the function of all cells and involve release of Ca 2+ from endoplasmic reticulum (ER) stores, triggering Ca 2+ entry through plasma membrane (PM) “store-operated channels” (SOCs). The identity of SOCs and their coupling to store depletion remain molecular and mechanistic mysteries. The single transmembrane-spanning Ca 2+ -binding protein, STIM1, is necessary in this coupling process and is proposed to function as an ER Ca 2+ sensor to provide the trigger for SOC activation. Here we reveal that, in addition to being an ER Ca 2+ sensor, STIM1 functions within the PM to control operation of the Ca 2+ entry channel itself. Increased expression levels of STIM1 correlate with a gain in function of Ca 2+ release-activated Ca 2+ (CRAC) channel activity. Point mutation of the N-terminal EF hand transforms the CRAC channel current ( I CRAC ) into a constitutively active, Ca 2+ store-independent mode. Mutants in the EF hand and cytoplasmic C terminus of STIM1 alter operational parameters of CRAC channels, including pharmacological profile and inactivation properties. Last, Ab externally applied to the STIM1 N-terminal EF hand blocks both I CRAC in hematopoietic cells and SOC-mediated Ca 2+ entry in HEK293 cells, revealing that STIM1 has an important functional presence within the PM. The results reveal that, in addition to being an ER Ca 2+ sensor, STIM1 functions within the PM to exert control over the operation of SOCs. As a cell surface signaling protein, STIM1 represents a key pharmacological target to control fundamental Ca 2+ -regulated processes including secretion, contraction, metabolism, cell division, and apoptosis.
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Cites
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STIM Is a Ca2+ Sensor Essential for Ca2+-Store-Depletion-Triggered Ca2+ Influx
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Cited by
Store-Operated Calcium Channels
Prakriya, M., & Lewis, R. S. (2015) · Physiological Reviews · doi:10.1152/physrev.00020.2014 · Cited by 1,239
Calcium signalling in lymphocyte activation and disease
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Molecular Basis of Calcium Signaling in Lymphocytes: STIM and ORAI
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STIM1 carboxyl-terminus activates native SOC, Icrac and TRPC1 channels
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CRACM1 Multimers Form the Ion-Selective Pore of the CRAC Channel
Vig, M., Beck, A., Billingsley, J. M., Lis, A., Parvez, S., Peinelt, C., Koomoa, D. L., Soboloff, J., Gill, D. L., Fleig, A., et al. (2006) · Current Biology · doi:10.1016/j.cub.2006.08.085 · Cited by 554
Self-citation
Metadata
- Authors
- Spassova, M. A., Soboloff, J., He, L.-P., Xu, W., Dziadek, M. A., & Gill, D. L.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2006-03-06
- Volume
- 103
- Issue
- 11
- Pages
- 4040-4045
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2069811868
- Cited by
- 306
- References
- 32
- FWCI
- 18.36
- Type
- journal article
- Language
- en
- Open access
- closed
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