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

作者：Gupta Kamlesh K^*; Alberico Emily O; Naethke Inke S; Goodson Holly V

来源：BioEssays, 2014, 36(9): 818-826.

DOI：10.1002/bies.201400029

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

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.

• 出版日期2014-9