Palmitoylation is a post-translational modification of Alix regulating the membrane organization of exosome-like small extracellular vesicles

Antonio Cupane, Mauro Manno, Samuele Raccosta, Antonietta Notaro, Stefano Caruso, Valentina Buffa, Ines Ferrara, Daniele P. Romancino, Agata Giallongo, Vincenzo Martorana, Rosina Noto, Antonella Bongiovanni, Alessandra D'Azzo, Yvan Campos

Risultato della ricerca: Article

2 Citazioni (Scopus)

Abstract

AbstractBackgroundVirtually all cell types have the capacity to secrete nanometer-sized extracellular vesicles, which have emerged in recent years as potent signal transducers and cell-cell communicators. The multifunctional protein Alix is a bona fide exosomal regulator and skeletal muscle cells can release Alix-positive nano-sized extracellular vesicles, offering a new paradigm for understanding how myofibers communicate within skeletal muscle and with other organs. S-palmitoylation is a reversible lipid post-translational modification, involved in different biological processes, such as the trafficking of membrane proteins, achievement of stable protein conformations, and stabilization of protein interactions.MethodsHere, we have used an integrated biochemical-biophysical approach to determine whether S-palmitoylation contributes to the regulation of extracellular vesicle production in skeletal muscle cells.ResultsWe ascertained that Alix is S-palmitoylated and that this post-translational modification influences its protein-protein interaction with CD9, a member of the tetraspanin protein family. Furthermore, we showed that the structural organization of the lipid bilayer of the small (nano-sized) extracellular vesicle membrane with altered palmitoylation is qualitatively different compared to mock control vesicles.ConclusionsWe propose that S-palmitoylation regulates the function of Alix in facilitating the interactions among extracellular vesicle-specific regulators and maintains the proper structural organization of exosome-like extracellular vesicle membranes.General SignificanceBeyond its biological relevance, our study also provides the means for a comprehensive structural characterization of EVs.
Lingua originaleEnglish
pagine (da-a)2879-2887
Numero di pagine9
RivistaBIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume1862
Stato di pubblicazionePublished - 2018

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Lipoylation
Exosomes
Post Translational Protein Processing
Membranes
Muscle
Skeletal Muscle
Proteins
Muscle Cells
Cells
Biological Phenomena
Protein Conformation
Lipid bilayers
Lipid Bilayers
Transducers
Conformations
Extracellular Vesicles
Membrane Proteins
Stabilization
Lipids

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cita questo

Palmitoylation is a post-translational modification of Alix regulating the membrane organization of exosome-like small extracellular vesicles. / Cupane, Antonio; Manno, Mauro; Raccosta, Samuele; Notaro, Antonietta; Caruso, Stefano; Buffa, Valentina; Ferrara, Ines; Romancino, Daniele P.; Giallongo, Agata; Martorana, Vincenzo; Noto, Rosina; Bongiovanni, Antonella; D'Azzo, Alessandra; Campos, Yvan.

In: BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, Vol. 1862, 2018, pag. 2879-2887.

Risultato della ricerca: Article

Cupane, A, Manno, M, Raccosta, S, Notaro, A, Caruso, S, Buffa, V, Ferrara, I, Romancino, DP, Giallongo, A, Martorana, V, Noto, R, Bongiovanni, A, D'Azzo, A & Campos, Y 2018, 'Palmitoylation is a post-translational modification of Alix regulating the membrane organization of exosome-like small extracellular vesicles', BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, vol. 1862, pagg. 2879-2887.
Cupane, Antonio ; Manno, Mauro ; Raccosta, Samuele ; Notaro, Antonietta ; Caruso, Stefano ; Buffa, Valentina ; Ferrara, Ines ; Romancino, Daniele P. ; Giallongo, Agata ; Martorana, Vincenzo ; Noto, Rosina ; Bongiovanni, Antonella ; D'Azzo, Alessandra ; Campos, Yvan. / Palmitoylation is a post-translational modification of Alix regulating the membrane organization of exosome-like small extracellular vesicles. In: BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS. 2018 ; Vol. 1862. pagg. 2879-2887.
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title = "Palmitoylation is a post-translational modification of Alix regulating the membrane organization of exosome-like small extracellular vesicles",
abstract = "AbstractBackgroundVirtually all cell types have the capacity to secrete nanometer-sized extracellular vesicles, which have emerged in recent years as potent signal transducers and cell-cell communicators. The multifunctional protein Alix is a bona fide exosomal regulator and skeletal muscle cells can release Alix-positive nano-sized extracellular vesicles, offering a new paradigm for understanding how myofibers communicate within skeletal muscle and with other organs. S-palmitoylation is a reversible lipid post-translational modification, involved in different biological processes, such as the trafficking of membrane proteins, achievement of stable protein conformations, and stabilization of protein interactions.MethodsHere, we have used an integrated biochemical-biophysical approach to determine whether S-palmitoylation contributes to the regulation of extracellular vesicle production in skeletal muscle cells.ResultsWe ascertained that Alix is S-palmitoylated and that this post-translational modification influences its protein-protein interaction with CD9, a member of the tetraspanin protein family. Furthermore, we showed that the structural organization of the lipid bilayer of the small (nano-sized) extracellular vesicle membrane with altered palmitoylation is qualitatively different compared to mock control vesicles.ConclusionsWe propose that S-palmitoylation regulates the function of Alix in facilitating the interactions among extracellular vesicle-specific regulators and maintains the proper structural organization of exosome-like extracellular vesicle membranes.General SignificanceBeyond its biological relevance, our study also provides the means for a comprehensive structural characterization of EVs.",
author = "Antonio Cupane and Mauro Manno and Samuele Raccosta and Antonietta Notaro and Stefano Caruso and Valentina Buffa and Ines Ferrara and Romancino, {Daniele P.} and Agata Giallongo and Vincenzo Martorana and Rosina Noto and Antonella Bongiovanni and Alessandra D'Azzo and Yvan Campos",
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T1 - Palmitoylation is a post-translational modification of Alix regulating the membrane organization of exosome-like small extracellular vesicles

AU - Cupane, Antonio

AU - Manno, Mauro

AU - Raccosta, Samuele

AU - Notaro, Antonietta

AU - Caruso, Stefano

AU - Buffa, Valentina

AU - Ferrara, Ines

AU - Romancino, Daniele P.

AU - Giallongo, Agata

AU - Martorana, Vincenzo

AU - Noto, Rosina

AU - Bongiovanni, Antonella

AU - D'Azzo, Alessandra

AU - Campos, Yvan

PY - 2018

Y1 - 2018

N2 - AbstractBackgroundVirtually all cell types have the capacity to secrete nanometer-sized extracellular vesicles, which have emerged in recent years as potent signal transducers and cell-cell communicators. The multifunctional protein Alix is a bona fide exosomal regulator and skeletal muscle cells can release Alix-positive nano-sized extracellular vesicles, offering a new paradigm for understanding how myofibers communicate within skeletal muscle and with other organs. S-palmitoylation is a reversible lipid post-translational modification, involved in different biological processes, such as the trafficking of membrane proteins, achievement of stable protein conformations, and stabilization of protein interactions.MethodsHere, we have used an integrated biochemical-biophysical approach to determine whether S-palmitoylation contributes to the regulation of extracellular vesicle production in skeletal muscle cells.ResultsWe ascertained that Alix is S-palmitoylated and that this post-translational modification influences its protein-protein interaction with CD9, a member of the tetraspanin protein family. Furthermore, we showed that the structural organization of the lipid bilayer of the small (nano-sized) extracellular vesicle membrane with altered palmitoylation is qualitatively different compared to mock control vesicles.ConclusionsWe propose that S-palmitoylation regulates the function of Alix in facilitating the interactions among extracellular vesicle-specific regulators and maintains the proper structural organization of exosome-like extracellular vesicle membranes.General SignificanceBeyond its biological relevance, our study also provides the means for a comprehensive structural characterization of EVs.

AB - AbstractBackgroundVirtually all cell types have the capacity to secrete nanometer-sized extracellular vesicles, which have emerged in recent years as potent signal transducers and cell-cell communicators. The multifunctional protein Alix is a bona fide exosomal regulator and skeletal muscle cells can release Alix-positive nano-sized extracellular vesicles, offering a new paradigm for understanding how myofibers communicate within skeletal muscle and with other organs. S-palmitoylation is a reversible lipid post-translational modification, involved in different biological processes, such as the trafficking of membrane proteins, achievement of stable protein conformations, and stabilization of protein interactions.MethodsHere, we have used an integrated biochemical-biophysical approach to determine whether S-palmitoylation contributes to the regulation of extracellular vesicle production in skeletal muscle cells.ResultsWe ascertained that Alix is S-palmitoylated and that this post-translational modification influences its protein-protein interaction with CD9, a member of the tetraspanin protein family. Furthermore, we showed that the structural organization of the lipid bilayer of the small (nano-sized) extracellular vesicle membrane with altered palmitoylation is qualitatively different compared to mock control vesicles.ConclusionsWe propose that S-palmitoylation regulates the function of Alix in facilitating the interactions among extracellular vesicle-specific regulators and maintains the proper structural organization of exosome-like extracellular vesicle membranes.General SignificanceBeyond its biological relevance, our study also provides the means for a comprehensive structural characterization of EVs.

UR - http://hdl.handle.net/10447/299023

M3 - Article

VL - 1862

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EP - 2887

JO - Biochimica et Biophysica Acta - General Subjects

JF - Biochimica et Biophysica Acta - General Subjects

SN - 0006-3002

ER -