Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2014 Apr 15;25(8):1298–1311. doi: 10.1091/mbc.E13-11-0687

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2014 Connolly et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

“ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology.

PMC Copyright notice

FIGURE 8: — Models for how MEI-1 contributes to pole focusing by severing microtubules, whereas ASPM-1 cross-links parallel microtubules and KLP-18 promotes bipolarity by cross-linking antiparallel microtubules. (A) MEI-1 may mediate spindle pole assembly by severing chromatin-nucleated microtubules. (B) KLP-18 may promote bipolarity by cross-linking antiparallel microtubules with the help of an unknown factor. ASPM-1 may focus spindle poles by cross-linking the minus ends of parallel microtubules through a dynein-dependent mechanism; consistent with this model, GFP:DHC-1 is nearly absent from meiotic spindles in mei-1(-) oocyte meiotic spindles (Supplemental Figure S3). The recruitment of ASPM-1 to oocyte meiotic spindle poles requires MEI-1; however, it is not known whether this recruitment involves a direct or indirect interaction, and hence this relationship is not depicted.