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

Marina Mapelli | Zendy; Cayetano González | Zendy

Open Access

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

Author(s) -

Marina Mapelli,

Cayetano González

Publication year - 2012

Publication title -

open biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.078

H-Index - 53

ISSN - 2046-2441

DOI - 10.1098/rsob.120102

Subject(s) - biology , polarity (international relations) , signal transducing adaptor protein , microbiology and biotechnology , spindle apparatus , mitosis , cell polarity , microtubule , cell division , cell , signal transduction , genetics

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.

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