Rapid NMR-scale purification of 15N,13C isotope-labeled recombinant human STIM1 coiled coil fragments

Rathner, Petr; Stadlbauer, Michael; Romanin, Christoph; Fahrner, Marc; Derler, Isabella; Müller, Norbert

doi:10.1016/j.pep.2018.01.013

Cited by 10 publications

(7 citation statements)

References 26 publications

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“…Structurally, all STIM1 monomers contain an N-terminal signal peptide, a canonical Ca 2+ -binding EF 1 hand, a non-Ca 2+binding EF 2 hand, and a sterile α-motif (SAM) domain in the ER luminal region (known as ER-SAM) (Dziadek and Johnstone, 2007;Schober et al, 2019). The C-terminus domain located in the cytosolic side of the ER membrane is characterized by the coiled-coil 1 (CC1) segments, a STIM-Orai-activating region (SOAR) or calcium release-activated calcium (CRAC) activation domain (CAD), and the motif S/TxIP which are the components of the Orai1 activation small fragment Stathopulos et al, 2013;Rathner et al, 2018; Figure 2).…”

Section: Store-operated Ca 2+ Entrymentioning

confidence: 99%

Relevance of Membrane Contact Sites in Cancer Progression

Gil-Hernández

Arroyo-Campuzano

Simoni‐Nieves

et al. 2021

Front. Cell Dev. Biol.

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Membrane contact sites (MCS) are typically defined as areas of proximity between heterologous or homologous membranes characterized by specific proteins. The study of MCS is considered as an emergent field that shows how crucial organelle interactions are in cell physiology. MCS regulate a myriad of physiological processes such as apoptosis, calcium, and lipid signaling, just to name a few. The membranal interactions between the endoplasmic reticulum (ER)–mitochondria, the ER–plasma membrane, and the vesicular traffic have received special attention in recent years, particularly in cancer research, in which it has been proposed that MCS regulate tumor metabolism and fate, contributing to their progression. However, as the therapeutic or diagnostic potential of MCS has not been fully revisited, in this review, we provide recent information on MCS relevance on calcium and lipid signaling in cancer cells and on its role in tumor progression. We also describe some proteins associated with MCS, like CERT, STIM1, VDAC, and Orai, that impact on cancer progression and that could be a possible diagnostic marker. Overall, these information might contribute to the understanding of the complex biology of cancer cells.

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Section: Store-operated Ca 2+ Entrymentioning

confidence: 99%

Relevance of Membrane Contact Sites in Cancer Progression

Gil-Hernández

Arroyo-Campuzano

Simoni‐Nieves

et al. 2021

Front. Cell Dev. Biol.

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“…The focus is on competitive interactions of cytosolic domains of STIM. The recently published functional data as well as structural data from nuclear magnetic resonance (NMR) spectroscopy and molecular dynamics (MD) simulations have been essential in advancing and complementing the characterization of STIM [15,21,22,30]. Moreover, we report results of ongoing functional investigations that are based on these novel NMR data.…”

Section: Introductionmentioning

confidence: 97%

STIM Proteins: An Ever-Expanding Family

Grabmayr

Romanin

Fahrner

2020

IJMS

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Stromal interaction molecules (STIM) are a distinct class of ubiquitously expressed single-pass transmembrane proteins in the endoplasmic reticulum (ER) membrane. Together with Orai ion channels in the plasma membrane (PM), they form the molecular basis of the calcium release-activated calcium (CRAC) channel. An intracellular signaling pathway known as store-operated calcium entry (SOCE) is critically dependent on the CRAC channel. The SOCE pathway is activated by the ligand-induced depletion of the ER calcium store. STIM proteins, acting as calcium sensors, subsequently sense this depletion and activate Orai ion channels via direct physical interaction to allow the influx of calcium ions for store refilling and downstream signaling processes. This review article is dedicated to the latest advances in the field of STIM proteins. New results of ongoing investigations based on the recently published functional data as well as structural data from nuclear magnetic resonance (NMR) spectroscopy and molecular dynamics (MD) simulations are reported and complemented with a discussion of the latest developments in the research of STIM protein isoforms and their differential functions in regulating SOCE.

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“…However, three point mutations were required because purification of the wild-type form was challenging (Yang et al, 2012). Very recently, Rathner et al reported an optimized protocol for one-step purification of cytosolic OASF ext (aa 234-491), which is similar to CC1-CAD-IDstim (Rathner et al, 2018). Thus, a structural study to demonstrate the intramolecular interaction of IDstim should be carried out in the near future.…”

Section: Discussionmentioning

confidence: 99%

The inactivation domain of STIM1 acts through intramolecular binding to the coiled-coil domain in the resting state

Lee

Jeong

et al. 2020

Journal of Cell Science

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Store-operated Ca 2+ entry (SOCE) is a major Ca 2+ influx pathway that is controlled by the ER Ca 2+ sensor STIM1. Abnormal activation of STIM1 directly influences Ca 2+ influx, resulting in severe diseases such as Stormorken syndrome. The inactivation domain of STIM1 (IDstim) has been identified as being essential for Ca 2+-dependent inactivation of STIM1 (CDI) after SOCE occurs. However, it is unknown whether IDstim is involved in keeping STIM1 inactive before CDI. Herein, we show that IDstim helps STIM1 keep inactive through intramolecular binding with the coiled-coil domain. Between IDstim and the coiled-coil domain, we found a short conserved linker whose extension or mutation leads to the constitutive activation of STIM1. We have demonstrated that IDstim needs the coiled-coil domain 1 (CC1) to inhibit the Ca 2+ release-activated Ca 2+ (CRAC) activation domain (CAD) activity and binds to a CC1-CAD fragment. Serial deletion of CC1 revealed that CC1α1 is a co-inhibitory domain of IDstim. CC1α1 deletion or leucine mutation, which abolishes the closed conformation, impaired the inhibitory effect and binding of IDstim. These results suggest that IDstim cooperates with CC1α1 to help STIM1 keep inactive under resting conditions.

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Rapid NMR-scale purification of 15N,13C isotope-labeled recombinant human STIM1 coiled coil fragments

Cited by 10 publications

References 26 publications

Relevance of Membrane Contact Sites in Cancer Progression

Relevance of Membrane Contact Sites in Cancer Progression

STIM Proteins: An Ever-Expanding Family

The inactivation domain of STIM1 acts through intramolecular binding to the coiled-coil domain in the resting state

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