Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 108, Issue 10, Pages 3988-3993Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1014758108
Keywords
Mal3; cytoskeleton; beryllium fluoride; EB1
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Funding
- European Molecular Biology Organization [ALTF 1032-2009]
- Human Frontier Science Program Organization [RGP0023/2008-C]
- National Center for Research Resources [P41-RR000592]
- National Institutes of Health [T32 GM-065103]
- Cancer Research UK [14256] Funding Source: researchfish
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Microtubule plus-end-tracking proteins (+TIPs) localize to growing microtubule plus ends to regulate a multitude of essential microtubule functions. End-binding proteins (EBs) form the core of this network by recognizing a distinct structural feature transiently existing in an extended region at growing microtubule ends and by recruiting other + TIPs to this region. The nature of the conformational difference allowing EBs to discriminate between tubulins in this region and other potential tubulin binding sites farther away from the microtubule end is unknown. By combining in vitro reconstitution, multicolor total internal reflection fluorescence microscopy, and electron microscopy, we demonstrate here that a closed microtubule B lattice with incorporated GTP.S, a slowly hydrolyzable GTP analog, can mimic the natural EB protein binding site. Our findings indicate that the guanine nucleotide.phosphate binding site is crucial for determining the affinity of EBs for lattice-incorporated tubulin. This defines the molecular mechanism by which EBs recognize growing microtubule ends.
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