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 Mar 1;29(5):610–621. doi: 10.1091/mbc.E17-06-0363

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

© 2018 Silkworth et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.

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.

PMC Copyright notice

FIGURE 1: — Delphilin is an actin assembly factor. (A) Domain structure of Delphilin. Green, PDZ domain; light blue, FH1 domain, with red proline-rich repeats; blue, FH2 domain. The numbering is based on mouse α-Delphilin (NP_579933.1). Constructs used in this paper are indicated below the diagram and shown in Supplemental Figure S1. All constructs were N-terminally His-tagged. (B) Pyrene–actin assembly assay with mDelFFC, concentrations as indicated (nM). (C) Pyrene–actin assembly assay with mDelFC, concentrations as indicated (nM). This construct is ∼15-fold weaker than mDelFFC. (D) Comparison of 150 nM wild-type mDelFC with point mutations in the same construct (I718A and K868A). (E) Comparison of actin assembly rates in pyrene assays with the indicated source of actin. Sequence similarities compared with human cytoplasmic actin are shown in parentheses. Conditions: A. castellani actin (4 μM, 10% pyrene labeled) was used in B–D. In E, the source of actin is indicated.