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    PITPNM1 phosphatidylinositol transfer protein membrane associated 1 [ Homo sapiens (human) ]

    Gene ID: 9600, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Attenuation of PITPNM1 Signaling Cascade Can Inhibit Breast Cancer Progression.

    Attenuation of PITPNM1 Signaling Cascade Can Inhibit Breast Cancer Progression.
    Liu Z, Shi Y, Lin Q, Yang W, Luo Q, Cen Y, Li J, Fang X, Jiang WG, Gong C., Free PMC Article

    01/15/2022
    Authors found that the phosphatidylinositol transfer protein Nir2 acts as an LTP and may replenish PI at the HCV RO by interacting with VAMP-associated proteins (VAPs), enabling continuous viral replication during chronic infection.

    Nir2 Is an Effector of VAPs Necessary for Efficient Hepatitis C Virus Replication and Phosphatidylinositol 4-Phosphate Enrichment at the Viral Replication Organelle.
    Wang H, Tai AW., Free PMC Article

    07/25/2020
    results suggest that Nir2 not only enhances EMT in vitro and breast cancer metastasis in animal models, but also contributes to breast cancer progression in human patients.

    The lipid-transfer protein Nir2 enhances epithelial-mesenchymal transition and facilitates breast cancer metastasis.
    Keinan O, Kedan A, Gavert N, Selitrennik M, Kim S, Karn T, Becker S, Lev S.

    09/5/2015
    Phosphatidic acid production triggers Phosphatidylinositol 4,5-Bisphosphate replenishment mediated by Nir2 and Nir3 at endoplasmic reticulum-plasma membrane junctions.

    Phosphatidylinositol 4,5-Bisphosphate Homeostasis Regulated by Nir2 and Nir3 Proteins at Endoplasmic Reticulum-Plasma Membrane Junctions.
    Chang CL, Liou J., Free PMC Article

    08/29/2015
    Nir2 translocates from the Golgi complex to the plasma membrane in response to GF stimulation.

    The phosphatidylinositol-transfer protein Nir2 binds phosphatidic acid and positively regulates phosphoinositide signalling.
    Kim S, Kedan A, Marom M, Gavert N, Keinan O, Selitrennik M, Laufman O, Lev S., Free PMC Article

    11/8/2014
    Results suggest a feedback mechanism that replenishes PM PIP2 during receptor-induced Ca(2+) signaling via the Ca(2+) effector E-Syt1 and the PITP Nir2 at ER-PM junctions.

    Feedback regulation of receptor-induced Ca2+ signaling mediated by E-Syt1 and Nir2 at endoplasmic reticulum-plasma membrane junctions.
    Chang CL, Hsieh TS, Yang TT, Rothberg KG, Azizoglu DB, Volk E, Liao JC, Liou J.

    08/30/2014
    A specific Thr residue in the Nir2 PI-transfer domain provides a regulatory site for targeting to lipid droplets. This may affect intracellular lipid trafficking & distribution & explain the dominant effect of the RdgB-T59E mutant on retinal degeneration.

    Targeting of Nir2 to lipid droplets is regulated by a specific threonine residue within its PI-transfer domain.
    Litvak V, Shaul YD, Shulewitz M, Amarilio R, Carmon S, Lev S.

    01/21/2010
    Nir2 is involved in maintaining a critical DAG pool in the Golgi apparatus by regulating its consumption via the CDP-choline pathway

    Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function.
    Litvak V, Dahan N, Ramachandran S, Sabanay H, Lev S.

    01/21/2010
    Phosphorylation of Nir2 by Cdk1 facilitates its dissociation from the Golgi apparatus, and phospho-Nir2 is localized in the cleavage furrow and midbody during cytokinesis.

    Mitotic phosphorylation of the peripheral Golgi protein Nir2 by Cdk1 provides a docking mechanism for Plk1 and affects cytokinesis completion.
    Litvak V, Argov R, Dahan N, Ramachandran S, Amarilio R, Shainskaya A, Lev S.

    01/21/2010
    Nir2, a human homolog of Drosophila melanogaster retinal degeneration B protein, is essential for cytokinesis.

    Nir2, a human homolog of Drosophila melanogaster retinal degeneration B protein, is essential for cytokinesis.
    Litvak V, Tian D, Carmon S, Lev S., Free PMC Article

    01/21/2010
    RdgB homologs play a preemptive role in excluding endogenous and exogenous modified purine deoxyribonucleoside triphosphates (dTNPs) from incorporation into DNA.

    Substrate specificity of RdgB protein, a deoxyribonucleoside triphosphate pyrophosphohydrolase.
    Burgis NE, Cunningham RP.

    01/21/2010
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