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Publication
Integrin-linked kinase promotes hepatic fat accumulation via F-actin
stabilization-dependent CD36 plasma membrane localization.
Authors Ghoshal K, Bock F, Winn NC, Printz RL, Bracy DP, Wasserman DH, Zent R, Pozzi A
Submitted By Submitted Externally on 8/26/2026
Status Published
Journal iScience
Year 2026
Date Published 8/21/2026
Volume : Pages 29 : 116610
PubMed Reference 42519009
Abstract Increased hepatic lipid accumulation occurs in high-fat diet (HFD)-induced
insulin resistance. Integrin-linked kinase (ILK) contributes to HFD-induced
hepatic insulin resistance by increasing hepatic triglyceride content. How ILK
promotes HFD-induced hepatic fatty acid accumulation is underexplored. ILK
favors the formation of F-actin bundling and is upregulated following HFD.
Moreover, the fatty acid transporter CD36 localizes to membrane ruffles rich in
F-actin following HFD. Thus, we investigated whether ILK-mediated F-actin
stabilization and liver fatty acid uptake are mechanistically linked. HFD-fed
mice lacking ILK in hepatocytes have reduced hepatic F-actin abundance, CD36
plasma membrane localization, and intracellular lipid accumulation. ILK-null
cells treated with the F-actin stabilizer jasplakinolide increased cortical
F-actin polymerization, plasma membrane-associated CD36, and intracellular lipid
uptake. CD36 inhibition reduced lipid uptake in jasplakinolide-treated ILK-null
cells, confirming that F-actin-induced CD36 plasma membrane localization
promotes lipid accumulation. Thus, ILK regulates intracellular lipid transport
by linking CD36 to an F-actin-rich cytoskeleton.




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