Journal
JOURNAL OF PHYSICS-CONDENSED MATTER
Volume 25, Issue 37, Pages -Publisher
IOP PUBLISHING LTD
DOI: 10.1088/0953-8984/25/37/374103
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Funding
- National Science Foundation (NSF) [CMMI-1242786, DBI-0923318, CMMI-0928540]
- MRSEC [DMR-0820506]
- Research Corporation for Science Advancement
- Div Of Civil, Mechanical, & Manufact Inn
- Directorate For Engineering [0928540] Funding Source: National Science Foundation
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Microtubules are rigid, proteinaceous filaments required to organize and rearrange the interior of cells. They organize space by two mechanisms, including acting as the tracks for long-distance cargo transporters, such as kinesin-1, and by forming a network that supports the shape of the cell. The microtubule network is composed of microtubules and a bevy of associated proteins and enzymes that self-organize using non-equilibrium dynamic processes. In order to address the effects of self-organization of microtubules, we have utilized the filament-gliding assay with kinesin-1 motors driving microtubule motion. To further enhance the complexity of the system and determine if new patterns are formed, we added the microtubule crosslinking protein MAP65-1. MAP65-1 is a microtubule-associated protein from plants that crosslinks antiparallel microtubules, similar to mammalian PRC1 and fission yeast Ase1. We find that MAP65 can slow and halt the velocity of microtubules in gliding assays, but when pre-formed microtubule bundles are added to gliding assays, kinesin-1 motors can pull apart the bundles and reconstitute cell-like protrusions.
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