Lrmp/Jaw1 is Expressed in Sweet, Bitter, and Umami Receptor-Expressing Cells

Shindo, Yoichiro; Kim, Mi-Ryung; Miura, Hirohito; Yuuki, Toshifumi; Kanda, Tomomasa; Hino, Akihiro; Kusakabe, Yuko

doi:10.1093/chemse/bjp097

Cited by 35 publications

(62 citation statements)

References 33 publications

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“…KASH5 expression appears limited to meiotic cells where it binds dynein to move chromosomes during homologous recombination 33,34 . Predominantly expressed in lymphocytes and taste cells, LRMP does not appear to interact with the cytoskeleton but instead binds to the calcium channel IP3 receptors 33,35 . There are multiple splice isoforms of nesprin 1 and nesprin 2 that do not contain the ONM-targeting KASH domain.…”

Section: Cytoskeletal Forces Are Exerted On the Nucleusmentioning

confidence: 99%

Nuclear Forces and Cell Mechanosensing

Alam

Lovett

Dickinson

et al. 2014

Progress in Molecular Biology and Translational Science

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Cells respond to mechanical signals, but the subcellular mechanisms are not well understood. The nucleus has recently emerged as an important mechanosensory organelle in the cell, as it is intimately connected to the cytoskeleton. Mechanical forces applied to cells that act on membrane-embedded receptors are transmitted through the cytoskeleton to the nuclear surface. Interfering with linkers of the nucleus to the cytoskeleton causes defects in cell mechanosensing and cell function. In this chapter, we discuss recent work in this area, highlighting the role that the nuclear linkages with the cytoskeleton play in cellular mechano-transduction.

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Section: Cytoskeletal Forces Are Exerted On the Nucleusmentioning

confidence: 99%

Nuclear Forces and Cell Mechanosensing

Alam

Lovett

Dickinson

et al. 2014

Progress in Molecular Biology and Translational Science

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“…Such discrepancy might be due to the tissue difference. Moreover, IP 3 Rs have three isoforms (IP 3 R1, IP 3 R2, and IP 3 R3) in mammals [30,31] and IP 3 R3 is the main receptor for mediating bitter tastant to induce Ca 2+ rise in taste cells [32]. Therefore, IP 3 R3 might play a similar role in chloroquine-triggered Ca 2+ increases in L6 cells.…”

Section: Discussionmentioning

confidence: 99%

Chloroquine Increases Glucose Uptake via Enhancing GLUT4 Translocation and Fusion with the Plasma Membrane in L6 Cells

Zhou

Yang

Xiong

et al. 2016

Cell Physiol Biochem

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Background/Aims: Chloroquine can induce an increase in the cellular uptake of glucose; however, the underlying mechanism is unclear. Methods: In this study, translocation of GLUT4 and intracellular Ca²⁺ changes were simultaneously observed by confocal microscope in L6 cells stably over-expressing IRAP-mOrange. The GLUT4 fusion with the plasma membrane (PM) was traced using HA-GLUT4-GFP. Glucose uptake was measured using a cell-based glucose uptake assay. GLUT4 protein was detected by Western blotting and mRNA level was detected by RT-PCR. Results: We found that chloroquine induced significant increases in glucose uptake, glucose transporter GLUT4 translocation to the plasma membrane (GTPM), GLUT4 fusion with the PM, and intracellular Ca²⁺ in L6 muscle cells. Chloroquine-induced increases of GTPM and intracellular Ca²⁺ were inhibited by Gallein (G_βγ inhibitor) and U73122 (PLC inhibitor). However, 2-APB (IP₃R blocker) only blocked the increase in intracellular Ca²⁺ but did not inhibit GTPM increase. These results indicate that chloroquine, via the G_βγ-PLC-IP₃-IP₃R pathway, induces elevation of Ca²⁺, and this Ca²⁺ increase does not play a role in chloroqui-ne-evoked GTPM increase. However, GLUT4 fusion with the PM and glucose uptake were significantly inhibited with BAPTA-AM. This suggests that Ca²⁺ enhances GLUT4 fusion with the PM resulting in glucose uptake increase. Conclusion: Our data indicate that chloroquine via G_βγ-PLC-IP₃-IP₃R induces Ca²⁺ elevation, which in turn promotes GLUT4 fusion with the PM. Moreover, chloroquine can enhance GLUT4 trafficking to the PM. These mechanisms eventually result in glucose uptake increase in control and insulin-resistant L6 cells. These findings suggest that chloroquine might be a potential drug for improving insulin tolerance in diabetic patients.

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“…Similar to KASH5, zebrafish LRMP contains several coiled-coil domains instead of spectrin repeats (Figs 1 and 2) (Lindeman and Pelegri, 2012;Horn et al, 2013). A second unusual mammalian KASH protein is mammalian LRMP (also known as Jaw1), which is also related to zebrafish LRMP, if by similarity of different domains (Shindo et al, 2010;Horn et al, 2013). It was originally described as an endoplasmic reticulum (ER) protein in lymphoid tissue (Behrens et al, 1994(Behrens et al, , 1996 and also interacts with the type III inositol 1,4,5-triphosphate receptor in taste buds (Shindo et al, 2010).…”

Section: Non-canonical Linc Complexes and Emerging Linc Complex Functmentioning

confidence: 99%

“…A second unusual mammalian KASH protein is mammalian LRMP (also known as Jaw1), which is also related to zebrafish LRMP, if by similarity of different domains (Shindo et al, 2010;Horn et al, 2013). It was originally described as an endoplasmic reticulum (ER) protein in lymphoid tissue (Behrens et al, 1994(Behrens et al, , 1996 and also interacts with the type III inositol 1,4,5-triphosphate receptor in taste buds (Shindo et al, 2010). Like for zebrafish LRMP, no SUN interactor is currently known.…”

Section: Non-canonical Linc Complexes and Emerging Linc Complex Functmentioning

confidence: 99%

LINCing the eukaryotic tree of life – towards a broad evolutionary comparison of nucleocytoplasmic bridging complexes

Meier

2016

Journal of Cell Science

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The nuclear envelope is much more than a simple barrier between nucleoplasm and cytoplasm. Nuclear envelope bridging complexes are protein complexes spanning both the inner and outer nuclear envelope membranes, thus directly connecting the cytoplasm with the nucleoplasm. In metazoans, they are involved in connecting the cytoskeleton with the nucleoskeleton, and act as anchoring platforms at the nuclear envelope for the positioning and moving of both nuclei and chromosomes. Recently, nucleocytoplasmic bridging complexes have also been identified in more evolutionarily diverse organisms, including land plants. Here, I discuss similarities and differences among and between eukaryotic supergroups, specifically of the proteins forming the cytoplasmic surface of these complexes. I am proposing a structure and function for a hypothetical ancestral nucleocytoplasmic bridging complex in the last eukaryotic common ancestor, with the goal to stimulate research in more diverse emerging model organisms.

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Lrmp/Jaw1 is Expressed in Sweet, Bitter, and Umami Receptor-Expressing Cells

Cited by 35 publications

References 33 publications

Nuclear Forces and Cell Mechanosensing

Nuclear Forces and Cell Mechanosensing

Chloroquine Increases Glucose Uptake via Enhancing GLUT4 Translocation and Fusion with the Plasma Membrane in L6 Cells

LINCing the eukaryotic tree of life – towards a broad evolutionary comparison of nucleocytoplasmic bridging complexes

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