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The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
Par6 is a key adaptor that links Cdc42 and atypical PKCs to Par3, and is implicated in the formation of normal tight junctions at epithelial cell–cell contacts. Expand
Exportin-5 mediates the nuclear export of pre-microRNAs and short hairpin RNAs.
It is demonstrated that human pre-miRNA nuclear export, and miRNA function, are dependent on Exportin-5, an additional cellular cofactor required for miRNA biogenesis and function. Expand
Structural insight into filament formation by mammalian septins.
The structures reveal a universal bipolar polymer building block, composed of an extended G domain, which forms oligomers and filaments by conserved interactions between adjacent nucleotide-binding sites and/or the amino- and carboxy-terminal extensions. Expand
Unconventional Rac-GEF activity is mediated through the Dock180–ELMO complex
A domain within Dock180 is identified that specifically recognizes nucleotide-free Rac and can mediate GTP loading of Rac in vitro and it is proposed that the Dock180–ELMO complex functions as an unconventional two-part exchange factor for Rac. Expand
Par-3 controls tight junction assembly through the Rac exchange factor Tiam1
It is shown that depletion of Par-3 in mammalian epithelial cells profoundly disrupts tight junction assembly, and a novel mechanism through which Par- 3 engages in the spatial regulation of Rac activity and establishment of epithelial polarity is revealed. Expand
Mammalian Pins Is a Conformational Switch that Links NuMA to Heterotrimeric G Proteins
It is proposed that a related switch mechanism might operate in asymmetric cell divisions in the fly and nematode by allowing LGN to interact simultaneously with both proteins, resulting in their cortical localization. Expand
Direct interaction of two polarity complexes implicated in epithelial tight junction assembly
The identification of a biochemical and functional link between these two complexes that is mediated by Par6 and PALS1 is highlighted, highlighting a previously unrecognized link between protein complexes that are essential for epithelial polarity and formation of tight junctions. Expand
The PAR proteins: fundamental players in animal cell polarization.
The par genes were discovered in genetic screens for regulators of cytoplasmic partitioning in the early embryo of C. elegans, and encode six different proteins required for asymmetric cell divisionExpand
Insulin-stimulated GLUT4 translocation requires the CAP-dependent activation of TC10
It is shown that phosphorylated Cbl recruits the CrkII–C3G complex to lipid rafts, where C3G specifically activates the small GTP-binding protein TC10, which is essential for insulin-stimulated glucose uptake and GLUT4 translocation. Expand
Parsing the Polarity Code
  • I. Macara
  • Biology, Medicine
  • Nature Reviews Molecular Cell Biology
  • 1 March 2004
An important goal is to decode — or parse — the molecular language of this network of proteins used throughout the Metazoa, which seems to function as components of a self-organizing network. Expand