Journal
BIOESSAYS
Volume 36, Issue 9, Pages 818-826Publisher
WILEY-BLACKWELL
DOI: 10.1002/bies.201400029
Keywords
APC; CLIP-170; EB1; light scattering assay; microtubule bundling; polymerization chaperone
Categories
Funding
- National Science Foundation Grants [NSF MCB-0951264, NSF MCB-1244593]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1244593] Funding Source: National Science Foundation
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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.
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