STIM Proteins and Regulation of SOCE in ER-PM Junctions

Ahmad, Moaz; Narayanasamy, Sasirekha; Ong, Hwei Ling; Ambudkar, Indu S.

doi:10.3390/biom12081152

Cited by 9 publications

(11 citation statements)

References 102 publications

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“…For example, the STIM1 puncta signal reshapes into annular structures when extended synaptogamines (E‐syt) relocate to the central area of these microdomains. Interestingly, E‐syt1 alone induces these ring‐shaped contacts; in contrast, STIM1 by itself can only generate the classical ER‐PMjs clusters 28 . Moreover, distances between the ER and the PM were different depending on the protein involved.…”

Section: Discussionmentioning

confidence: 98%

“…Interestingly, E-syt1 alone induces these ring-shaped contacts; in contrast, STIM1 by itself can only generate the classical ER-PMjs clusters. 28 Moreover, distances between the ER and the PM were different depending on the protein involved. This finding suggests that different proteins generate different types of ER-PMjs, morphologically and functionally, as both promote different calcium responses.…”

Section: Discussionmentioning

confidence: 99%

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Routing of Kv7.1 to endoplasmic reticulum plasma membrane junctions

Serrano‐Novillo,

Estadella,

Navarro‐Pérez

et al. 2024

Acta Physiologica

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AimThe voltage‐gated Kv7.1 channel, in association with the regulatory subunit KCNE1, contributes to the IKs current in the heart. However, both proteins travel to the plasma membrane using different routes. While KCNE1 follows a classical Golgi‐mediated anterograde pathway, Kv7.1 is located in endoplasmic reticulum‐plasma membrane junctions (ER‐PMjs), where it associates with KCNE1 before being delivered to the plasma membrane.MethodsTo characterize the channel routing to these spots we used a wide repertoire of methodologies, such as protein expression analysis (i.e. protein association and biotin labeling), confocal (i.e. immunocytochemistry, FRET, and FRAP), and dSTORM microscopy, transmission electron microscopy, proteomics, and electrophysiology.ResultsWe demonstrated that Kv7.1 targeted ER‐PMjs regardless of the origin or architecture of these structures. Kv2.1, a neuronal channel that also contributes to a cardiac action potential, and JPHs, involved in cardiac dyads, increased the number of ER‐PMjs in nonexcitable cells, driving and increasing the level of Kv7.1 at the cell surface. Both ER‐PMj inducers influenced channel function and dynamics, suggesting that different protein structures are formed. Although exhibiting no physical interaction, Kv7.1 resided in more condensed clusters (ring‐shaped) with Kv2.1 than with JPH4. Moreover, we found that VAMPs and AMIGO, which are Kv2.1 ancillary proteins also associated with Kv7.1. Specially, VAP B, showed higher interaction with the channel when ER‐PMjs were stimulated by Kv2.1.ConclusionOur results indicated that Kv7.1 may bind to different structures of ER‐PMjs that are induced by different mechanisms. This variable architecture can differentially affect the fate of cardiac Kv7.1 channels.

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Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

Routing of Kv7.1 to endoplasmic reticulum plasma membrane junctions

Serrano‐Novillo,

Estadella,

Navarro‐Pérez

et al. 2024

Acta Physiologica

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“…The ER is a calcium‐ion storage and unique protein synthesis mechanism that is distributed throughout neurons with the presence of multiple domains associated with different functions. One such domain is called EMC, which is located on the ER membrane 63,64 . The location of ER/EMC within neurons reveals their contribution to synaptic plasticity by regulating various cellular processes from protein synthesis to Ca 2+ signaling.…”

Section: The Functions Of Emcmentioning

confidence: 99%

ER membrane complex (EMC): Structure, functions, and roles in diseases

Zhu,

Zhang

2024

The FASEB Journal

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The endoplasmic reticulum (ER) is the largest membrane system in eukaryotic cells and is the primary site for the biosynthesis of lipids and carbohydrates, as well as for the folding, assembly, modification, and transport of secreted and integrated membrane proteins. The ER membrane complex (EMC) on the ER membrane is an ER multiprotein complex that affects the quality control of membrane proteins, which is abundant and widely preserved. Its disruption has been found to affect a wide range of processes, including protein and lipid synthesis, organelle communication, endoplasmic reticulum stress, and viral maturation, and may lead to neurodevelopmental disorders and cancer. Therefore, EMC has attracted the attention of many scholars and become a hot field. In this paper, we summarized the main contributions of the research of EMC in the past nearly 15 years, and reviewed the structure and function of EMC as well as its related diseases. We hope this review will promote further progress of research on EMC.

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“…We conclude that ESYT1mediated MERC tethering is required for efficient ER to mitochondria Ca 2+ transfer. ER-PM contact sites are responsible for store-operated Ca 2+ entry (SOCE) (Ahmad, Narayanasamy et al 2022). It has been suggested that ESYT1 ER-PM tethering would be activated by and reinforce SOCE (Giordano, Saheki et al 2013, Maleth, Choi et al 2014, Idevall-Hagren, Lu et al 2015, Kang, Zhou et al 2019.…”

Section: Esyt1 Is Required For Er To Mitochondria Ca 2+ Transfermentioning

confidence: 99%

ESYT1 tethers the endoplasmic reticulum to mitochondria and is required for mitochondrial lipid and calcium homeostasis

Janer

Morris

Krols

et al. 2022

Preprint

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Mitochondria interact with the endoplasmic reticulum (ER) at structurally and functionally specialized membrane contact sites known as mitochondria-ER contact sites (MERCs). MERCs are crucial for a myriad of physiological functions including lipid synthesis and transport, and calcium signaling. Alterations in the structure, composition or regulation of MERCs contribute to the aetiology of many pathologies including neurodegenerative and metabolic diseases. The proteins mediating the formation of MERCs have been extensively studied in yeast, where the ER-mitochondria encounter structure (ERMES) complex mediates the transport of lipids between the ER and mitochondria via three lipid binding SMP-domain proteins. However, none of the SMP proteins of the ERMES complex have orthologues in mammals suggesting that alternate pathways have evolved in metazoans. Combining proximity labelling (BioID), confocal microscopy and subcellular fractionation, we found that the ER resident SMP-domain containing protein ESYT1 was enriched at MERCs, where it forms a complex with the outer mitochondrial membrane protein SYNJ2BP. The deletion of ESYT1 or SYNJ2BP reduced the number and length of MERCs, indicating that the ESYT1-SYN2JBP complex plays a role in tethering ER and mitochondria. Loss of this complex impaired ER to mitochondria calcium flux and provoked a significant alteration of the mitochondrial lipidome, most prominently a reduction of cardiolipins and phosphatidylethanolamines. Both phenotypes were rescued by re-expression of wild-type ESYT1 as well as an artificial mitochondria-ER tether. Together, these results reveal a novel function of ESYT1 in mitochondrial and cellular homeostasis through its role in the regulation of MERCs.

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STIM Proteins and Regulation of SOCE in ER-PM Junctions

Cited by 9 publications

References 102 publications

Routing of Kv7.1 to endoplasmic reticulum plasma membrane junctions

Routing of Kv7.1 to endoplasmic reticulum plasma membrane junctions

ER membrane complex (EMC): Structure, functions, and roles in diseases

ESYT1 tethers the endoplasmic reticulum to mitochondria and is required for mitochondrial lipid and calcium homeostasis

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