288 results found
    1. Biochemistry and Chemical Biology
    2. Cancer Biology

    Identification of PARP-7 substrates reveals a role for MARylation in microtubule control in ovarian cancer cells

    Lavanya H Palavalli Parsons et al.
    PARP-7 is a mono(ADP-ribosyl) transferase that directs an extensive ADP-ribosylated proteome to control microtubule stability, and regulate ovarian cancer cell growth and motility.
    1. Cancer Biology
    2. Cell Biology

    Blockade of the LRP16-PKR-NF-κB signaling axis sensitizes colorectal carcinoma cells to DNA-damaging cytotoxic therapy

    Xiaolei Li et al.
    Leukemia-Related Protein 16 (LRP16), a member of the macro domain family, plays a crucial role in orchestrating genotoxicity-initiated NF-κB signaling in the colon and the pathophysiological relevance of NF-κB activation induced by LRP16 in colonic cell survival/recovery from extrinsic DNA damage.
    1. Biochemistry and Chemical Biology

    Chemical genetics and proteome-wide site mapping reveal cysteine MARylation by PARP-7 on immune-relevant protein targets

    Kelsie M Rodriguez et al.
    A combined chemical genetics, proximity labeling, and ADP-ribose site mapping approach shows that PARP-7 mono-ADP-ribosylates immune-relevant proteins on cysteine amino acids.
    1. Biochemistry and Chemical Biology

    LARP1 functions as a molecular switch for mTORC1-mediated translation of an essential class of mRNAs

    Sungki Hong et al.
    LARP1 turns off and on the translation of an essential class of mRNAs by acting as a key effecter and regulator for mTORC1.
    1. Cell Biology
    2. Plant Biology

    Parallel global profiling of plant TOR dynamics reveals a conserved role for LARP1 in translation

    M Regina Scarpin et al.
    Plants and humans use a shared mechanism, the eukaryotic metabolic sensor TARGET OF RAPAMYCIN protein kinase and its substrate, an RNA-binding protein called LARP1, to coordinate post-transcriptional gene expression.
    1. Cancer Biology
    2. Cell Biology

    PARP1 inhibitors trigger innate immunity via PARP1 trapping-induced DNA damage response

    Chiho Kim et al.
    Identification of PARP1 trapping as the major contributor of PARP1 inhibitor-induced innate immune response.
    1. Cell Biology

    In vivo vizualisation of mono-ADP-ribosylation by dPARP16 upon amino-acid starvation

    Angelica Aguilera-Gomez et al.
    Amino-acid induced Sec body formation is mediated by PARP16 dependent MARylation of Sec16, a component of the endoplasmic reticulum exit site.
    1. Biochemistry and Chemical Biology

    HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase

    Johannes Rudolph et al.
    The polymerase activity of PARP1 is converted to hydrolase activity upon binding of Histone Parylation Factor 1 (HPF1) with nucleosome activators.
    1. Chromosomes and Gene Expression

    PARP1-dependent recruitment of the FBXL10-RNF68-RNF2 ubiquitin ligase to sites of DNA damage controls H2A.Z loading

    Gergely Rona et al.
    Upon genotoxic stress, the FBXL10-RNF68-RNF2 ubiquitin ligase complex mono-ubiquitylates histone H2A and mediates H2A/H2A.Z exchange to repress transcription and ensures proper high fidelity homologous recombination repair.
    1. Cell Biology
    2. Microbiology and Infectious Disease

    Coupling chemosensory array formation and localization

    Alejandra Alvarado et al.
    Formation and cell pole-localization of chemotactic signaling-arrays is a coupled process mediated by ParP, which drives localized array-assembly and regulates the localization-dynamics of its network constituents.

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