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Bioessays. 2014 Sep;36(9):818-26. doi: 10.1002/bies.201400029. Epub 2014 Jun 18.

Promoting microtubule assembly: A hypothesis for the functional significance of the +TIP network.

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Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, USA.


Regulation of microtubule (MT) dynamics is essential for many cellular processes, but the machinery that controls MT dynamics remains poorly understood. MT plus-end tracking proteins (+TIPs) are a set of MT-associated proteins that dynamically track growing MT ends and are uniquely positioned to govern MT dynamics. +TIPs associate with each other in a complex array of inter- and intra-molecular interactions known as the "+TIP network." Why do so many +TIPs bind to other +TIPs? Typical answers include the ideas that these interactions localize proteins where they are needed, deliver proteins to the cortex, and/or create regulatory pathways. We propose an additional and more mechanistic hypothesis: that +TIPs bind each other to create a superstructure that promotes MT assembly by constraining the structural fluctuations of the MT tip, thus acting as a polymerization chaperone.


APC; CLIP-170; EB1; light scattering assay; microtubule bundling; polymerization chaperone

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