期刊
MOLECULAR CELL
卷 43, 期 3, 页码 418-431出版社
CELL PRESS
DOI: 10.1016/j.molcel.2011.07.011
关键词
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资金
- National High Technology Research Program [2006AA02A320]
- National Major Basic Research Program [2009CB918600, 2011CB808505]
- National Science Foundation of China [30970574, 20973040, 31070642]
- Shanghai Rising-Star Program [10QA1400700]
- Science and Technology Commission of Shanghai Municipality [08DZ2270500]
- Shanghai Leading Academic Discipline Project [8108]
- National Institute of Health [GM079506]
- American Cancer Society [RSG0717601CSM]
- RGC [663808, 664009, 660709, 663610, HKUST6/CRF/10, SEG_HKUST06, AoE/B-15/01-II, AoE/M-04/04]
Asymmetric cell division requires the establishment of cortical cell polarity and the orientation of the mitotic spindle along the axis of cell polarity. Evidence from invertebrates demonstrates that the Par3/Par6/aPKC and NuMA/LGN/G alpha i complexes, which are thought to be physically linked by the adaptor protein mInscuteable (mInsc), play indispensable roles in this process. However, the molecular basis for the binding of LGN to NuMA and mInsc is poorly understood. The high-resolution structures of the LGN/NuMA and LGN/mInsc complexes presented here provide mechanistic insights into the distinct and highly specific interactions of the LGN TPRs with mInsc and NuMA. Structural comparisons, together with biochemical and cell biology studies, demonstrate that the interactions of NuMA and mInsc with LGN are mutually exclusive, with mInsc binding preferentially. Our results suggest that the Par3/mInsc/LGN and NuMA/LGN/G alpha i complexes play sequential and partially overlapping roles in asymmetric cell division.
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