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

. 2022 Nov 10;10(11):2884. doi: 10.3390/biomedicines10112884

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

© 2022 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

PMC Copyright notice

PVAT control vascular function by mean of precise mechanism related to adiponectin-dependent AMPK activation. Two conditions are relevant. (A) non-stimulated with no link between adiponectin (APN) and Adiponectin receptor 1 (AdipoR1). Adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 1 (APPL1) do not work alongside protein phosphatase 2A (PP2A). Protein kinase Cζ (PKCζ) induces phosphorylation of liver kinase B 1 (LKB1) affecting its translocation to the nucleus. (B) The stimulated state induces the bind of APN to AdipoR1 with activation of APPL1 resulting in PKCζ dephosphorylation by P. Dephosphorylated PKCζ is no longer effective to phosphorylate LKB1. PP2A also dephosphorylates LKB1, which results in LKB1 translocation to the cytoplasm. LKB1 phosphorylates AMP-activated protein kinase (AMPK) in the form of the AdipoR1/APPL1/PP2A/ PKCζ/LKB1 complex. Abbreviations are in the text.