Structural basis for interaction between the conserved cell polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched protein (LGN)

Interaction between the mammalian cell polarity proteins mInsc (mammalian homologue of Inscuteable) and Leu-Gly-Asn repeat-enriched protein (LGN), as well as that between their respective Drosophila homologues Inscuteable and Partner of Inscuteable (Pins), plays crucial roles in mitotic spindle orie...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2011-11, Vol.108 (48), p.19210-19215
Hauptverfasser:	Yuzawa, Satoru, Kamakura, Sachiko, Iwakiri, Yuko, Hayase, Junya, Sumimoto, Hideki
Format:	Artikel
Sprache:	eng
Schlagworte:	Adaptor Proteins, Signal Transducing - chemistry Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Biological Sciences Carrier Proteins - metabolism Cell division cell polarity Cell Polarity - physiology Cells Chromatography, Gel COS cells crystal structure Crystallization Drosophila Fluorescence G-proteins HeLa cells Humans Immunoprecipitation Insects Intracellular Signaling Peptides and Proteins - genetics Intracellular Signaling Peptides and Proteins - metabolism Mammals Mitotic spindle apparatus Models, Molecular Mutagenesis mutants Mutation Neuroblasts Neuroglia Neurons Protein Conformation Proteins Spindle Apparatus - physiology Surface Plasmon Resonance Ultracentrifugation
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