Cross-talk between N-terminal and C-terminal domains in stromal interaction molecule 2 (STIM2) determines enhanced STIM2 sensitivity Article Swipe
Scott M. Emrich
,
Ryan E. Yoast
,
Ping Xin
,
Xuexin Zhang
,
Trayambak Pathak
,
Robert M. Nwokonko
,
Maxime Guéguinou
,
Krishna Prasad Subedi
,
Yandong Zhou
,
Indu S. Ambudkar
,
Nadine Hempel
,
Khaled Machaca
,
Donald L. Gill
,
Mohamed Trebak
·
YOU?
·
· 2019
· Open Access
·
· DOI: https://doi.org/10.1074/jbc.ra118.006801
YOU?
·
· 2019
· Open Access
·
· DOI: https://doi.org/10.1074/jbc.ra118.006801
Store-operated Ca2+ entry (SOCE) is a ubiquitous pathway for Ca2+ influx across the plasma membrane (PM). SOCE is mediated by the endoplasmic reticulum (ER)-associated Ca2+-sensing proteins stromal interaction molecule 1 (STIM1) and STIM2, which transition into an active conformation in response to ER Ca2+ store depletion, thereby interacting with and gating PM-associated ORAI1 channels. Although structurally homologous, STIM1 and STIM2 generate distinct Ca2+ signatures in response to varying strengths of agonist stimulation. The physiological functions of these Ca2+ signatures, particularly under native conditions, remain unclear. To investigate the structural properties distinguishing STIM1 and STIM2 activation of ORAI1 channels under native conditions, here we used CRISPR/Cas9 to generate STIM1-/-, STIM2-/-, and STIM1/2-/- knockouts in HEK293 and colorectal HCT116 cells. We show that depending on cell type, STIM2 can significantly sustain SOCE in response to maximal store depletion. Utilizing the SOCE modifier 2-aminoethoxydiphenyl borate (2-APB), we demonstrate that 2-APB-activated store-independent Ca2+ entry is mediated exclusively by endogenous STIM2. Using variants that either stabilize or disrupt intramolecular interactions of STIM C termini, we show that the increased flexibility of the STIM2 C terminus contributes to its selective store-independent activation by 2-APB. However, STIM1 variants with enhanced flexibility in the C terminus failed to support its store-independent activation. STIM1/STIM2 chimeric constructs indicated that coordination between N-terminal sensitivity and C-terminal flexibility is required for specific store-independent STIM2 activation. Our results clarify the structural determinants underlying activation of specific STIM isoforms, insights that are potentially useful for isoform-selective drug targeting.
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Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1074/jbc.ra118.006801
- http://www.jbc.org/article/S0021925820362906/pdf
- OA Status
- hybrid
- Cited By
- 45
- References
- 62
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W2920743482
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W2920743482Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1074/jbc.ra118.006801Digital Object Identifier
- Title
-
Cross-talk between N-terminal and C-terminal domains in stromal interaction molecule 2 (STIM2) determines enhanced STIM2 sensitivityWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2019Year of publication
- Publication date
-
2019-03-02Full publication date if available
- Authors
-
Scott M. Emrich, Ryan E. Yoast, Ping Xin, Xuexin Zhang, Trayambak Pathak, Robert M. Nwokonko, Maxime Guéguinou, Krishna Prasad Subedi, Yandong Zhou, Indu S. Ambudkar, Nadine Hempel, Khaled Machaca, Donald L. Gill, Mohamed TrebakList of authors in order
- Landing page
-
https://doi.org/10.1074/jbc.ra118.006801Publisher landing page
- PDF URL
-
https://www.jbc.org/article/S0021925820362906/pdfDirect link to full text PDF
- Open access
-
YesWhether a free full text is available
- OA status
-
hybridOpen access status per OpenAlex
- OA URL
-
https://www.jbc.org/article/S0021925820362906/pdfDirect OA link when available
- Concepts
-
STIM1, ORAI1, Cell biology, Chemistry, HEK 293 cells, Biophysics, Endoplasmic reticulum, Gating, Gene isoform, Neuroscience, Biology, Biochemistry, Receptor, GeneTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
45Total citation count in OpenAlex
- Citations by year (recent)
-
2025: 5, 2024: 5, 2023: 7, 2022: 8, 2021: 9Per-year citation counts (last 5 years)
- References (count)
-
62Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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