The involvement of ankyrin in the regulation of inositol 1,4,5-trisphosphate receptor-mediated internal Ca2+ release from Ca2+ storage vesicles in mouse T-lymphoma cells.

Bourguignon, Lilly Y.W.; Jin, Hengtao; Iida, Naoko; Brandt, Neil R.; Zhang, She Hui

doi:10.1016/s0021-9258(18)53175-6

Cited by 154 publications

(16 citation statements)

References 58 publications

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“…Which type of interaction is involved in the segregation of the Ins(1,4,5)P $ receptor in a special region beneath the PM ? The Ins(1,4,5)P $ receptor interacts with the cytoskeletal proteins ankyrin or actin in such different tissues as the cerebellum, mouse T-lymphoma cells or the liver [27,60,61]. In the present work, the Ins(1,4,5)P $ receptor was localized beneath the PM, along the canalicular domain and to a lesser extent along the sinusoidal domain.…”

Section: Discussionsupporting

confidence: 50%

Intracellular calcium stores and inositol 1,4,5-trisphosphate receptor in rat liver cells

Lièvremont

Hill

Tran

et al. 1996

Biochemical Journal

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The D-myo-inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] receptor was localized by immunofluorescence experiments in situ in liver cryosections. Two anti-Ins(1,4,5)P3 receptor antibodies (against the 14 C-terminal residues of the type 1 receptor or against the entire cerebellar receptor) weakly decorated the whole cytoplasm, and a more intense labelling was observed at the periphery of the hepatocytes, particularly beneath the canalicular and the sinusoidal domains of the plasma membrane (PM). Antibodies against calreticulin, the Ca2+ pump (SERCA2b) or endoplasmic reticulum (ER) membranes homogeneously labelled the cytoplasm and the subplasmalemmal area. These data indicate that the ER can be divided into at least two specialized subregions: one is located throughout most of the cytoplasm and contains markers of the rough ER (RER), calreticulin, SERCA2b and a low density of Ins(1,4,5)P3 receptor, and the other is confined to the periphery of the cells and contains calreticulin, Ca2+ pump, RER markers and a high density of Ins(1,4,5)P3 receptor. A membrane fraction enriched in Ins(1,4,5)P3 receptor and in markers of the PM was immuno-adsorbed with the antibody against the C-terminal end of the Ins(1,4,5)P3 receptor and pelleted with Sepharose protein A. The immuno-isolated material was enriched in Ins(1,4,5)P3 receptor, but none of the markers of the ER or of the PM could be detected. This suggests that the Ins(1,4,5)P3 receptor is localized on discrete domains of the ER membrane beneath the canalicular and the sinusoidal membranes, where it was found at higher densities than the other markers.

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Section: Discussionsupporting

confidence: 50%

Intracellular calcium stores and inositol 1,4,5-trisphosphate receptor in rat liver cells

Lièvremont

Hill

Tran

et al. 1996

Biochemical Journal

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“…Membrane fractionation of keratinocytes was carried out as described (Bourguignon et al, 1993) with modifications. Briefly, NHKs were suspended in cold homogenizing buffer (20 mM HEPES, pH 7.4, 2 mM EDTA, 1 mM dithiothreitol) supplemented with Complete protease inhibitors (Roche Diagnostics, Indianapolis, IN), and were homogenized with Polytron homogenizer at 27,000 r.p.m., 41C for 30 seconds.…”

Section: Membrane Fractionationmentioning

confidence: 99%

The Role of the Calcium Sensing Receptor in Regulating Intracellular Calcium Handling in Human Epidermal Keratinocytes

Chang

Bikle

2007

Journal of Investigative Dermatology

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Calcium is critical for controlling the balance of proliferation and differentiation in epidermal keratinocytes. We previously reported that the calcium sensing receptor (CaR) is required for mediating Ca2+ signaling and extracellular Ca2+ (Ca2+(o))-induced differentiation. In this study, we investigated the mechanism by which CaR regulates intracellular Ca2+ (Ca2+(i)) and its role in differentiation. Membrane fractionation, fluorescence immunolocalization, and co-immunoprecipitation studies were performed to assess potential interactions between CaR and other regulators of Ca2+ stores and channels. We found that the glycosylated form of CaR forms a complex with phospholipase C gamma1, IP3 receptor (IP3R), and the Golgi Ca2+-ATPase, secretory pathway Ca2+-ATPase 1, in the trans-Golgi. Inactivation of the endogenous CaR gene by adenoviral expression of a CaR antisense cDNA inhibited Ca2+(i) response to Ca2+(o), decreased Ca2+(i) stores, decreased Ca2+(o)-induced differentiation, but augmented store-operated channel activity and Ca2+ uptake by intracellular organelles. Our results indicate that CaR regulates keratinocyte differentiation in part by modulating Ca2+(i) stores via interactions with Ca2+ pumps and channels that regulate those stores.

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“…4, A and B). At the early time of chase (0 min), ␣ and ␤ were recovered from the denser region of the gradient, reflecting a status where ␤ subunits, shortly after synthesis, are devoid of ␥ subunits, but they still fractionate with large dense particles, such as the cytosolic ribosomes on which they are synthesized (7). At the 20-min chase point we noted a movement of ␤ and ␣ subunits towards lower density fractions (B, C, and D interface).…”

Section: Distribution Of G ␣ and G ␤ Subunits Assessed By Subcellular Fractionationmentioning

confidence: 99%

Assembly and Intracellular Targeting of the βγ Subunits of Heterotrimeric G Proteins

Rehm

Ploegh

1997

The Journal of Cell Biology

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The assembly in living cells of heterotrimeric guanine nucleotide binding proteins from their constituent α, β, and γ subunits is a complex process, compounded by the multiplicity of the genes that encode them, and the diversity of receptors and effectors with which they interact. Monoclonal anti-β antibodies (ARC5 and ARC9), raised against immunoaffinity purified βγ complexes, recognize β subunits when not associated with γ and can thus be used to monitor assembly of βγ complexes. Complex formation starts immediately after synthesis and is complete within 30 min. Assembly occurs predominantly in the cytosol, and association of βγ complexes with the plasma membrane fraction starts between 15–30 min of chase. Three pools of β subunits can be distinguished based on their association with γ subunits, their localization, and their detergent solubility. Association of β and α subunits with detergent-insoluble domains occurs within 1 min of chase, and increases to reach a plateau of near complete detergent resistance within 30 min of chase. Brefeldin A treatment does not interfere with delivery of βγ subunits to detergent-insoluble domains, suggesting that assembly of G protein subunits with their receptors occurs distally from the BFA-imposed block of intracellular membrane trafficking and may occur directly at the plasma membrane.

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The involvement of ankyrin in the regulation of inositol 1,4,5-trisphosphate receptor-mediated internal Ca2+ release from Ca2+ storage vesicles in mouse T-lymphoma cells.

Cited by 154 publications

References 58 publications

Intracellular calcium stores and inositol 1,4,5-trisphosphate receptor in rat liver cells

Intracellular calcium stores and inositol 1,4,5-trisphosphate receptor in rat liver cells

The Role of the Calcium Sensing Receptor in Regulating Intracellular Calcium Handling in Human Epidermal Keratinocytes

Assembly and Intracellular Targeting of the βγ Subunits of Heterotrimeric G Proteins

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