The Drosophila microtubule-associated protein mars stabilizes mitotic spindles by crosslinking microtubules through its N-terminal region

PLoS One. 2013 Apr 4;8(4):e60596. doi: 10.1371/journal.pone.0060596. Print 2013.

Abstract

Correct segregation of genetic material relies on proper assembly and maintenance of the mitotic spindle. How the highly dynamic microtubules (MTs) are maintained in stable mitotic spindles is a key question to be answered. Motor and non-motor microtubule associated proteins (MAPs) have been reported to stabilize the dynamic spindle through crosslinking adjacent MTs. Mars, a novel MAP, is essential for the early development of Drosophila embryos. Previous studies showed that Mars is required for maintaining an intact mitotic spindle but did not provide a molecular mechanism for this function. Here we show that Mars is able to stabilize the mitotic spindle in vivo. Both in vivo and in vitro data reveal that the N-terminal region of Mars functions in the stabilization of the mitotic spindle by crosslinking adjacent MTs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Animals, Genetically Modified
  • Blastoderm / metabolism
  • Cell Nucleus / metabolism
  • Drosophila / embryology
  • Drosophila / genetics
  • Drosophila / metabolism*
  • Drosophila Proteins
  • Gene Expression
  • Genes, Lethal
  • Microtubule-Associated Proteins / chemistry
  • Microtubule-Associated Proteins / metabolism*
  • Microtubules / metabolism*
  • Mutation
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism*
  • Protein Binding
  • Protein Stability
  • Protein Transport
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • SAP90-PSD95 Associated Proteins
  • Spindle Apparatus / genetics
  • Spindle Apparatus / metabolism*

Substances

  • Drosophila Proteins
  • Mars protein, Drosophila
  • Microtubule-Associated Proteins
  • Nerve Tissue Proteins
  • Recombinant Fusion Proteins
  • SAP90-PSD95 Associated Proteins

Grant support

This work was funded by the Deutsche Forschungsgemeinschaft (Cluster of Excellence and DFG Research Center Nanoscale Microscopy and Molecular Physiology of the Brain; DFG Research Group 1756). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.