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

. 2019 Jan 29;10:483. doi: 10.1038/s41467-019-08317-8

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

© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Fig. 6 — Mechanism of IRSp53 regulation by 14-3-3. a 14-3-3 inhibits membrane binding of pIRSp53. The relative abundances of WT IRSp53-FLAG and mutant M234-FLAG in the cytosolic (black bars) and membrane fractions (gray bars) of fed and serum-starved HEK293T cells, were determined by weighting the abundance of IRSp53 or M234 against the combined abundance of GAPDH and β-actin, for the cytosolic fraction, or E-cadherin, for the membrane fraction. Error bars are ± s.d. from three different transfections and two experiments per transfection (shown as open circles). The statistical significance of the measurements was determined using an unpaired two-sided Student’s t-test (n.s., non-significant; **p < 0.01; ***p < 0.001; ****p < 0.0001). b Model of IRSp53 activation and phosphorylation-dependent inhibition by 14-3-3. IRSp53 is activated by the binding of Cdc42 to the CRIB-PR domain and/or cytoskeletal effectors to the SH3 domain. Activation exposes the I-BAR domain for binding to the plasma membrane. Phosphorylation of IRSp53 and subsequent binding of 14-3-3 to phosphorylation sites located between the CRIB-PR and SH3 domains stabilizes the autoinhibited conformation and inhibits the binding of Cdc42 and downstream cytoskeletal effectors