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

. 2018 Sep 3;217(9):3019–3029. doi: 10.1083/jcb.201707081

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

© 2018 Wynne and Vallee

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).

PMC Copyright notice

Figure 3. — Nde1 Cdk1 phosphorylation of Nde1 enhances CENP-F interaction. (A) Diagram showing CENP-F fragment used for biochemical analysis (NBD: amino acids 2,122–2,297). (B) GST-CENP-F NBD pull-down of GPF-Nde1 constructs from HeLa cells demonstrates increased binding of GFP-phosphomimetic Nde1. (C) GST-CENP-F NBD pull-down of bacterially expressed HA-Nde1 after in vitro phosphorylation with recombinant Cdk1/CyclinB. Levels of Nde1 in the CENP-F NBD pull-downs were quantified and again revealed an increased binding of Cdk1-phosphorylated Nde1 to the GST CENP-F NBD fragment. (D) Anti-GFP immunoprecipitation of endogenous CENP-F with GFP-tagged Nde1 phosphorylation state constructs. Immunoprecipitation of GFP WT Nde1 and GFP-Nde1-3E each specially coprecipitated endogenous CENP-F. Mean ± SEM of three independent experiments is represented. **, P < 0.005; *, P < 0.05.