Profiling calcium-dependent interactions between Sorcin and intrinsically disordered regions of human proteome
| Autor: | Theo Battista, Gianni Colotti, Andrea Ilari, Andrea Carotti, Ylva Ivarsson, Ilaria Genovese, Annarita Fiorillo |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Phage display Proteome Protein subunit Calcium pump Biophysics Biochemistry Protein–protein interaction Sorcin 03 medical and health sciences 0302 clinical medicine Protein-protein interaction Short linear motif Human proteome project Humans Glucose homeostasis Proteomic peptide phage display (ProP-PD) Molecular Biology Chemistry Endoplasmic reticulum Calcium-Binding Proteins Cell biology Intrinsically Disordered Proteins 030104 developmental biology 030220 oncology & carcinogenesis Calcium HeLa Cells |
| Zdroj: | Biochimica et biophysica acta. G, General subjects 1864 (2020). doi:10.1016/j.bbagen.2020.129618 info:cnr-pdr/source/autori:Genovese, Ilaria; Carotti, Andrea; Ilari, Andrea; Fiorillo, Annarita; Battista, Theo; Colotti, Gianni; Ivarsson, Ylva/titolo:Profiling calcium-dependent interactions between Sorcin and intrinsically disordered regions of human proteome/doi:10.1016%2Fj.bbagen.2020.129618/rivista:Biochimica et biophysica acta. G, General subjects (Print)/anno:2020/pagina_da:/pagina_a:/intervallo_pagine:/volume:1864 |
| DOI: | 10.1016/j.bbagen.2020.129618 |
| Popis: | Background Sorcin is a calcium sensor that exerts many calcium-related functions in the cells, e.g. it regulates calcium concentration in the cytoplasm, endoplasmic reticulum (ER) and mitochondria, by interacting with calcium pumps, exchangers and channels. Albeit Sorcin is an interesting potential cancer target, little is known about its interactors upon calcium-mediated activation. Our previous study suggested that Sorcin may recognize short linear binding motifs as the crystal structure revealed a self-interaction with a GYYPGG stretch in its N-terminus, and combinatorial peptide-phage display provided support for peptide-mediated interactions. Methods In this study we screened for motif-based interactions between Sorcin and intrinsically disordered regions of the human proteome using proteomic peptide phage display (ProP-PD). We identified a peptide belonging to protein phosphatase 1 regulatory subunit 3G (PPP1R3G) as a potential novel interactor and confirm the interaction through biophysical and cell-based approaches, and provide structural information through molecular dynamics simulations. Results Altogether, we identify a preferred motif in the enriched pool of binders and a peptide belonging to protein phosphatase 1 regulatory subunit 3G (PPP1R3G) as a preferred ligand. Conclusion Through this study we gain information on a new Sorcin binding partner and profile Sorcin's motif-based interaction. General significance The interaction between Sorcin and PPP1R3G may suggest a close dependence between glucose homeostasis and calcium concentration in the different cell compartments, opening a completely new and interesting scenery yet to be fully disclosed. |
| Databáze: | OpenAIRE |
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