Proteins that associate with microtubules (MTs) are crucial to generate MT arrays and establish different cellular architectures. One example is PRC1 (protein regulator of cytokinesis 1), which cross-links antiparallel MTs and is essential for the completion of mitosis and cytokinesis. Here we describe a 4-Å-resolution cryo-EM structure of monomeric PRC1 bound to MTs. Residues in the spectrin domain of PRC1 contacting the MT are highly conserved and interact with the same pocket recognized by kinesin. We additionally found that PRC1 promotes MT assembly even in the presence of the MT stabilizer taxol. Interestingly, the angle of the spectrin domain on the MT surface corresponds to the previously observed cross-bridge angle between MTs cross-linked by full-length, dimeric PRC1. This finding, together with molecular dynamic simulations describing the intrinsic flexibility of PRC1, suggests that the MT-spectrin domain interface determines the geometry of the MT arrays cross-linked by PRC1.

Original languageEnglish
Pages (from-to)9430-9
Number of pages10
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number34
Publication statusPublished - 23 Aug 2016
Externally publishedYes


  • Amino Acid Motifs
  • Animals
  • Binding Sites
  • Cell Cycle Proteins/genetics
  • Cryoelectron Microscopy
  • Crystallography, X-Ray
  • Gene Expression
  • Humans
  • Kinesin/genetics
  • Microtubules/metabolism
  • Molecular Dynamics Simulation
  • Paclitaxel/chemistry
  • Protein Binding
  • Protein Conformation, alpha-Helical
  • Protein Conformation, beta-Strand
  • Protein Interaction Domains and Motifs
  • Protein Multimerization
  • Protein Subunits/chemistry
  • Recombinant Proteins/genetics
  • Swine
  • Tubulin/genetics
  • Tubulin Modulators/chemistry


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