Send to

Choose Destination
See comment in PubMed Commons below
Open Biol. 2012 Aug;2(8):120102. doi: 10.1098/rsob.120102.

On the inscrutable role of Inscuteable: structural basis and functional implications for the competitive binding of NuMA and Inscuteable to LGN.

Author information

  • 1Department of Experimental Oncology, European Institute of Oncology, Via Adamello 16, 20139 Milan, Italy.


Alignment of the mitotic spindle to the cellular polarity axis is a prerequisite for asymmetric cell divisions. The protein network coordinating the spindle position with cortical polarity includes the molecular machinery pulling on astral microtubules, which is assembled on conserved NuMA:LGN:Gαi complexes, the polarity proteins Par3:Par6:aPKC and an adaptor molecule known as Inscuteable (Insc). To date, all these components were assumed to enter a macromolecular complex localized at polarity sites in mitosis. However, recent structural studies revealed the Insc and NuMA are mutually exclusive interactors of LGN, implying that the molecular mechanism of spindle coupling to polarity is more sophisticated than has been believed to date.


asymmetric cell division; spindle orientation; structural biology

[PubMed - indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk