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Collin T. McManus on Muck Rack

Collin T. McManus

As seen in: Nature, PLOS, BioRxiv
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Articles

Molecular insight into microtubule nucleation by the XMAP215/γ-TuRC module

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By Collin T. McManus, Sophie M. Travis, Philip Jeffrey, Rui Zhang, Sabine Petry
| Nature Verified
Abstract It has become increasingly evident in recent years that nucleation of microtubules from a diverse set of microtubule organizing centers (MTOCs) requires both the γ-tubulin ring complex (γ-TuRC) and the microtubule polymerase XMAP215. Despite their essentiality, little is known about how these nucleation factors interact and work together to generate microtubules.
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Mechanism of how the universal module XMAP215 γ-TuRC nucleates microtubules

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By Collin T. McManus, Sophie M. Travis, Philip Jeffrey, Rui Zhang
| BioRxiv
Abstract It has become increasingly evident in recent years that nucleation of microtubules from a diverse set of MTOCs requires both the γ-tubulin ring complex (γ-TuRC) and the microtubule polymerase XMAP215. Despite their essentiality, little is known about how these nucleation factors interact and work together to generate microtubules.
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Mutagenesis and structural modeling implicate RME-8 IWN domains as conformational control points

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By Anne H. Norris, New jersey, Biochemistry Rutgers, Collin T. McManus
| PLOS
The role of SNX-1 We have previously proposed that SNX-1 is a positive regulator of RME-8 as loss of either SNX-1 or RME-8 has similar effects on cargo recycling and expansion of the degradative microdomain [2]. Our model predicts that SNX-1 binding derepresses RME-8, allowing RME-8 to uncoat both ESCRT-0 and, intriguingly, SNX-1 itself.
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