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 Aug 17;9:3303. doi: 10.1038/s41467-018-05812-2

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

© The Author(s) 2018

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. 8 — A model for SENP1-mediated VEGFR2 trafficking. SENP1 maintains VEGFR2 in an un-SUMOylated state, ensuring normal trafficking of VEGFR2 from ER/Golgi to plasma membrane in EC. We propose that a pool of VEGFR2 is constantly SUMOylated by an unidentified SUMO E3 ligase in resting EC or upon VEGF-engagement, and stored at the Golgi. Under pathological conditions such as ischemia, SENP1 expression is induced so that SUMOylated VEGFR2 can be rapidly deconjugated and transported to plasma membrane for strong angiogenesis response. Pathological conditions such as hyperglycemia and diabetes downregulate/inactivate SENP1, causing VEGFR2 hyper-SUMOylation and impaired angiogenic signalling as seen in SENP1-deficient EC (see text for details)