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

TY - JOUR

T1 - Promoting microtubule assembly

T2 - a hypothesis for the functional significance of the +TIP network

AU - Gupta, Kamlesh K.

AU - Alberico, Emily O.

AU - Nathke, Inke S.

AU - Goodson, Holly V.

N1 - © 2014 WILEY Periodicals, Inc.

PY - 2014/9

Y1 - 2014/9

N2 - 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. +TIPs are a set of microtubule-associated proteins that dynamically track growing microtubule plus-ends and are considered master controllers of microtubule dynamics. Here, we propose that the network of interactions between +TIPs creates a superstructure that promotes microtubule assembly by constraining the structural fluctuations of the microtubule tips.

AB - 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. +TIPs are a set of microtubule-associated proteins that dynamically track growing microtubule plus-ends and are considered master controllers of microtubule dynamics. Here, we propose that the network of interactions between +TIPs creates a superstructure that promotes microtubule assembly by constraining the structural fluctuations of the microtubule tips.

UR - https://www.scopus.com/pages/publications/84905923153

U2 - 10.1002/bies.201400029

DO - 10.1002/bies.201400029

M3 - Article

C2 - 24943963

SN - 0265-9247

VL - 36

SP - 818

EP - 826

JO - BioEssays

JF - BioEssays

IS - 9

ER -