Recruitment of TNF ligands to lipid rafts is mediated by their physical association with caveolin-1.

Autor: Glukhova XA; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Puschino, Russia., Trizna JA; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Puschino, Russia., Melnik BS; Institute of Protein Research, Russian Academy of Sciences, Puschino, Russia., Proussakova OV; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Puschino, Russia., Beletsky IP; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Puschino, Russia.
Jazyk: angličtina
Zdroj: FEBS letters [FEBS Lett] 2022 Jan; Vol. 596 (2), pp. 211-218. Date of Electronic Publication: 2021 Dec 20.
DOI: 10.1002/1873-3468.14257
Abstrakt: Activities of the tumour necrosis factor (TNF) family members are associated with their targeting to lipid rafts, specialised regions of the plasma membrane. Herein, we investigated the physical association of TNF and its family members cluster of differentiation 40 ligand (CD40L) and tumour necrosis factor-related apoptosis-inducing ligand with caveolin-1, a lipid raft resident protein. We discovered that the intracellular domains of TNF and CD40L interact with caveolin-1, and the membrane proximal region of TNF is required for the binding of caveolin-1 domains. Full-length TNF can form a complex with caveolin-1 in membrane rafts of HeLa cells, and caveolin-1 knockdown leads to impaired TNF transport to rafts. These findings provide the first evidence of a direct interaction between TNF, CD40L and caveolin-1 and suggest that caveolin-1 may be responsible for recruiting TNF to lipid rafts.
(© 2021 Federation of European Biochemical Societies.)
Databáze: MEDLINE
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