Sökning: onr:"swepub:oai:DiVA.org:uu-414938" >
Profiling calcium-d...
Profiling calcium-dependent interactions between Sorcin and intrinsically disordered regions of human proteome
-
- Genovese, Ilaria (författare)
- Uppsala universitet,Biokemi,Univ Ferrara, Dept Med Sci, Lab Technol Adv Therapies LTTA, Via Fossato di Mortara 70, I-44121 Ferrara, Italy.;Univ Sapienza, Dept Biochem Sci, Ple Aldo Moro 5, I-00185 Rome, Italy.
-
- Carotti, Andrea (författare)
- Univ Perugia, Dept Pharmaceut Sci, Via Fabretti 48, I-06123 Perugia, Italy.
-
- Ilari, Andrea (författare)
- Univ Sapienza, Inst Mol Biol & Pathol, Dept Biochem Sci, IBPM CNR,Natl Res Council, Ple Aldo Moro 5, I-00185 Rome, Italy.
-
visa fler...
-
- Fiorillo, Annarita (författare)
- Univ Sapienza, Dept Biochem Sci, Ple Aldo Moro 5, I-00185 Rome, Italy.
-
- Battista, Theo (författare)
- Univ Sapienza, Dept Biochem Sci, Ple Aldo Moro 5, I-00185 Rome, Italy.
-
- Colotti, Gianni (författare)
- Univ Sapienza, Inst Mol Biol & Pathol, Dept Biochem Sci, IBPM CNR,Natl Res Council, Ple Aldo Moro 5, I-00185 Rome, Italy.
-
- Ivarsson, Ylva (författare)
- Uppsala universitet,Biokemi
-
visa färre...
-
(creator_code:org_t)
- Elsevier, 2020
- 2020
- Engelska.
-
Ingår i: Biochimica et Biophysica Acta - General Subjects. - : Elsevier. - 0304-4165 .- 1872-8006. ; 1864:8
- Relaterad länk:
-
https://urn.kb.se/re...
-
visa fler...
-
https://doi.org/10.1...
-
visa färre...
Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Läkemedelskemi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Medicinal Chemistry (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- Protein-protein interaction
- Short linear motif
- Proteomic peptide phage display (ProP-PD)
- Sorcin
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas