Journal: Molecular Cell

Abbreviation

Mol Cell

Publisher

Cell Press

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ISSN

1097-2765
1097-4164

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Publications1 - 10 of 97
  • The Mechanism of Prion Inhibition by HET-S
    Item type: Journal Article
    Greenwald, Jason; Buhtz, Carolin; Ritter, Christiane; et al. (2010)
    Molecular Cell
  • Digital quantification of proteins and mRNA in single mammalian cells
    Item type: Journal Article
    Albayrak, Cem; Jordi, Christian A.; Zechner, Christoph; et al. (2016)
    Molecular Cell
  • Impact of MicroRNA Levels, Target-Site Complementarity, and Cooperativity on Competing Endogenous RNA-Regulated Gene Expression
    Item type: Journal Article
    Denzler, Rémy; McGeary, Sean E.; Title, Alexandra C.; et al. (2016)
    Molecular Cell
    Expression changes of competing endogenous RNAs (ceRNAs) have been proposed to influence microRNA (miRNA) activity and thereby regulate other transcripts containing miRNA-binding sites. Here, we find that although miRNA levels define the extent of repression, they have little effect on the magnitude of the ceRNA expression change required to observe derepression. Canonical 6-nt sites, which typically mediate modest repression, can nonetheless compete for miRNA binding, with potency ∼20% of that observed for canonical 8-nt sites. In aggregate, low-affinity/background sites also contribute to competition. Sites with extensive additional complementarity can appear as more potent, but only because they induce miRNA degradation. Cooperative binding of proximal sites for the same or different miRNAs does increase potency. These results provide quantitative insights into the stoichiometric relationship between miRNAs and target abundance, target-site spacing, and affinity requirements for ceRNA-mediated gene regulation, and the unusual circumstances in which ceRNA-mediated gene regulation might be observed.
  • Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases
    Item type: Journal Article
    Buljan, Marija; Ciuffa, Rodolfo; van Drogen, Audrey; et al. (2020)
    Molecular Cell
    Protein kinases are essential for signal transduction and control of most cellular processes, including metabolism, membrane transport, motility, and cell cycle. Despite the critical role of kinases in cells and their strong association with diseases, good coverage of their interactions is available for only a fraction of the 535 human kinases. Here, we present a comprehensive mass-spectrometry-based analysis of a human kinase interaction network covering more than 300 kinases. The interaction dataset is a high-quality resource with more than 5,000 previously unreported interactions. We extensively characterized the obtained network and were able to identify previously described, as well as predict new, kinase functional associations, including those of the less well-studied kinases PIM3 and protein O-mannose kinase (POMK). Importantly, the presented interaction map is a valuable resource for assisting biomedical studies. We uncover dozens of kinase-disease associations spanning from genetic disorders to complex diseases, including cancer.
  • Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control
    Item type: Journal Article
    Molinari, Maurizio; Eriksson, Klara Kristin; Calanca, Verena; et al. (2004)
    Molecular Cell
  • Sequence and chromatin features guide DNA double-strand break resection initiation
    Item type: Journal Article
    Gnügge, Robert; Reginato, Giordano; Cejka, Petr; et al. (2023)
    Molecular Cell
    DNA double-strand breaks (DSBs) are cytotoxic genome lesions that must be accurately and efficiently repaired to ensure genome integrity. In yeast, the Mre11-Rad50-Xrs2 (MRX) complex nicks 5′-terminated DSB ends to initiate nucleolytic processing of DSBs for repair by homologous recombination. How MRX-DNA interactions support 5′ strand-specific nicking and how nicking is influenced by the chromatin context have remained elusive. Using a deep sequencing-based assay, we mapped MRX nicks at single-nucleotide resolution next to multiple DSBs in the yeast genome. We observed that the DNA end-binding Ku70-Ku80 complex directed DSB-proximal nicks and that repetitive MRX cleavage extended the length of resection tracts. We identified a sequence motif and a DNA meltability profile that is preferentially nicked by MRX. Furthermore, we found that nucleosomes as well as transcription impeded MRX incisions. Our findings suggest that local DNA sequence and chromatin features shape the activity of this central DSB repair complex.
  • Yeast Sporulation and [SMAUG+] Prion: Faster Is Not Always Better
    Item type: Journal Article
    Parfenova, Iuliia; Barral, Yves (2020)
    Molecular Cell
  • The TFIIH Subunit Tfb3 Regulates Cullin Neddylation
    Item type: Journal Article
    Rabut, Gwénaël; Le Dez, Gaelle; Verma, Rati; et al. (2011)
    Molecular Cell
  • Mechanistic Insights into Autoinhibition of the Oncogenic Chromatin Remodeler ALC1
    Item type: Journal Article
    Lehmann, Laura C.; Hewitt, Graeme; Aibara, Shintaro; et al. (2017)
    Molecular Cell
    Human ALC1 is an oncogene-encoded chromatin-remodeling enzyme required for DNA repair that possesses a poly(ADP-ribose) (PAR)-binding macro domain. Its engagement with PARylated PARP1 activates ALC1 at sites of DNA damage, but the underlying mechanism remains unclear. Here, we establish a dual role for the macro domain in autoinhibition of ALC1 ATPase activity and coupling to nucleosome mobilization. In the absence of DNA damage, an inactive conformation of the ATPase is maintained by juxtaposition of the macro domain against predominantly the C-terminal ATPase lobe through conserved electrostatic interactions. Mutations within this interface displace the macro domain, constitutively activate the ALC1 ATPase independent of PARylated PARP1, and alter the dynamics of ALC1 recruitment at DNA damage sites. Upon DNA damage, binding of PARylated PARP1 by the macro domain induces a conformational change that relieves autoinhibitory interactions with the ATPase motor, which selectively activates ALC1 remodeling upon recruitment to sites of DNA damage.
  • Dcn1 Functions as a Scaffold-Type E3 Ligase for Cullin Neddylation
    Item type: Journal Article
    Kurz, Thimo; Chou, Yang-Chieh; Willems, Andrew R.; et al. (2008)
    Molecular Cell
Publications1 - 10 of 97