Proteasome Activity Is Affected by Fluctuations in Insulin-Degrading Enzyme Distribution

Diego Sbardella; Grazia Raffaella Tundo; Francesca Sciandra; Manuela Bozzi; Magda Gioia; Chiara Ciaccio; Umberto Tarantino; Andrea Brancaccio; Massimo Coletta; Stefano Marini

doi:10.1371/journal.pone.0132455

Proteasome Activity Is Affected by Fluctuations in Insulin-Degrading Enzyme Distribution

Diego Sbardella, Grazia Raffaella Tundo, Francesca Sciandra, Manuela Bozzi, Magda Gioia, Chiara Ciaccio, Umberto Tarantino, Andrea Brancaccio, Massimo Coletta, Stefano Marini

School of Biochemistry

Research output: Contribution to journal › Article (Academic Journal) › peer-review

23 Citations (Scopus)

313 Downloads (Pure)

Abstract

Insulin-Degrading-Enzyme (IDE) is a Zn²⁺-dependent peptidase highly conserved throughout evolution and ubiquitously distributed in mammalian tissues wherein it displays a prevalent cytosolic localization. We have recently demonstrated a novel Heat Shock Protein-like behaviour of IDE and its association with the 26S proteasome. In the present study, we examine the mechanistic and molecular features of IDE-26S proteasome interaction in a cell experimental model, extending the investigation also to the effect of IDE on the enzymatic activities of the 26S proteasome. Further, kinetic investigations indicate that the 26S proteasome activity undergoes a functional modulation by IDE through an extra-catalytic mechanism. The IDE-26S proteasome interaction was analyzed during the Heat Shock Response and we report novel findings on IDE intracellular distribution that might be of critical relevance for cell metabolism.

Original language	English
Article number	e0132455
Number of pages	21
Journal	PLoS ONE
Volume	10
Issue number	7
DOIs	https://doi.org/10.1371/journal.pone.0132455
Publication status	Published - 17 Jul 2015

Keywords

Blotting, Western
Cell Line, Tumor
Complex Mixtures
Endoplasmic Reticulum
Gene Silencing
Heat-Shock Response
Humans
Insulysin
Neuroblastoma
Proteasome Endopeptidase Complex
Protein Binding
Stress, Physiological
Subcellular Fractions
Time Factors
Journal Article
Research Support, Non-U.S. Gov't

Access to Document

10.1371/journal.pone.0132455

Full-text PDF (final published version)
This is the final published version of the article (version of record). It first appeared online via Public Library of Science at http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0132455. Please refer to any applicable terms of use of the publisher.
Final published version, 1.66 MBLicence: CC BY

Handle.net

Persistent link

Cite this

@article{21cfb021b9d34745b117507f54903250,

title = "Proteasome Activity Is Affected by Fluctuations in Insulin-Degrading Enzyme Distribution",

abstract = "Insulin-Degrading-Enzyme (IDE) is a Zn2+-dependent peptidase highly conserved throughout evolution and ubiquitously distributed in mammalian tissues wherein it displays a prevalent cytosolic localization. We have recently demonstrated a novel Heat Shock Protein-like behaviour of IDE and its association with the 26S proteasome. In the present study, we examine the mechanistic and molecular features of IDE-26S proteasome interaction in a cell experimental model, extending the investigation also to the effect of IDE on the enzymatic activities of the 26S proteasome. Further, kinetic investigations indicate that the 26S proteasome activity undergoes a functional modulation by IDE through an extra-catalytic mechanism. The IDE-26S proteasome interaction was analyzed during the Heat Shock Response and we report novel findings on IDE intracellular distribution that might be of critical relevance for cell metabolism.",

keywords = "Blotting, Western, Cell Line, Tumor, Complex Mixtures, Endoplasmic Reticulum, Gene Silencing, Heat-Shock Response, Humans, Insulysin, Neuroblastoma, Proteasome Endopeptidase Complex, Protein Binding, Stress, Physiological, Subcellular Fractions, Time Factors, Journal Article, Research Support, Non-U.S. Gov't",

author = "Diego Sbardella and Tundo, {Grazia Raffaella} and Francesca Sciandra and Manuela Bozzi and Magda Gioia and Chiara Ciaccio and Umberto Tarantino and Andrea Brancaccio and Massimo Coletta and Stefano Marini",

year = "2015",

month = jul,

day = "17",

doi = "10.1371/journal.pone.0132455",

language = "English",

volume = "10",

journal = "PLoS ONE",

issn = "1932-6203",

publisher = "Public Library of Science",

number = "7",

}

TY - JOUR

T1 - Proteasome Activity Is Affected by Fluctuations in Insulin-Degrading Enzyme Distribution

AU - Sbardella, Diego

AU - Tundo, Grazia Raffaella

AU - Sciandra, Francesca

AU - Bozzi, Manuela

AU - Gioia, Magda

AU - Ciaccio, Chiara

AU - Tarantino, Umberto

AU - Brancaccio, Andrea

AU - Coletta, Massimo

AU - Marini, Stefano

PY - 2015/7/17

Y1 - 2015/7/17

N2 - Insulin-Degrading-Enzyme (IDE) is a Zn2+-dependent peptidase highly conserved throughout evolution and ubiquitously distributed in mammalian tissues wherein it displays a prevalent cytosolic localization. We have recently demonstrated a novel Heat Shock Protein-like behaviour of IDE and its association with the 26S proteasome. In the present study, we examine the mechanistic and molecular features of IDE-26S proteasome interaction in a cell experimental model, extending the investigation also to the effect of IDE on the enzymatic activities of the 26S proteasome. Further, kinetic investigations indicate that the 26S proteasome activity undergoes a functional modulation by IDE through an extra-catalytic mechanism. The IDE-26S proteasome interaction was analyzed during the Heat Shock Response and we report novel findings on IDE intracellular distribution that might be of critical relevance for cell metabolism.

AB - Insulin-Degrading-Enzyme (IDE) is a Zn2+-dependent peptidase highly conserved throughout evolution and ubiquitously distributed in mammalian tissues wherein it displays a prevalent cytosolic localization. We have recently demonstrated a novel Heat Shock Protein-like behaviour of IDE and its association with the 26S proteasome. In the present study, we examine the mechanistic and molecular features of IDE-26S proteasome interaction in a cell experimental model, extending the investigation also to the effect of IDE on the enzymatic activities of the 26S proteasome. Further, kinetic investigations indicate that the 26S proteasome activity undergoes a functional modulation by IDE through an extra-catalytic mechanism. The IDE-26S proteasome interaction was analyzed during the Heat Shock Response and we report novel findings on IDE intracellular distribution that might be of critical relevance for cell metabolism.

KW - Blotting, Western

KW - Cell Line, Tumor

KW - Complex Mixtures

KW - Endoplasmic Reticulum

KW - Gene Silencing

KW - Heat-Shock Response

KW - Humans

KW - Insulysin

KW - Neuroblastoma

KW - Proteasome Endopeptidase Complex

KW - Protein Binding

KW - Stress, Physiological

KW - Subcellular Fractions

KW - Time Factors

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1371/journal.pone.0132455

DO - 10.1371/journal.pone.0132455

M3 - Article (Academic Journal)

C2 - 26186340

VL - 10

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 7

M1 - e0132455

ER -

Proteasome Activity Is Affected by Fluctuations in Insulin-Degrading Enzyme Distribution

Abstract

Keywords

Access to Document

Handle.net

Fingerprint

Cite this