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Microtubules and Microtubule-Associated Proteins
Author(s) -
Holly V. Goodson,
Erin M. Jonasson
Publication year - 2018
Publication title -
cold spring harbor perspectives in biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.011
H-Index - 173
ISSN - 1943-0264
DOI - 10.1101/cshperspect.a022608
Subject(s) - biology , microtubule , microtubule associated protein , microbiology and biotechnology
Microtubules act as "railways" for motor-driven intracellular transport, interact with accessory proteins to assemble into larger structures such as the mitotic spindle, and provide an organizational framework to the rest of the cell. Key to these functions is the fact that microtubules are "dynamic." As with actin, the polymer dynamics are driven by nucleotide hydrolysis and influenced by a host of specialized regulatory proteins, including microtubule-associated proteins. However, microtubule turnover involves a surprising behavior-termed dynamic instability-in which individual polymers switch stochastically between growth and depolymerization. Dynamic instability allows microtubules to explore intracellular space and remodel in response to intracellular and extracellular cues. Here, we review how such instability is central to the assembly of many microtubule-based structures and to the robust functioning of the microtubule cytoskeleton.

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