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Structural basis of Sorcin-mediated calcium-dependent signal transduction
Univ Roma La Sapienza, CNR, Inst Mol Biol & Pathol, I-00185 Rome, Italy.;Univ Roma La Sapienza, Dept Biochem Sci, I-00185 Rome, Italy..
Univ Roma La Sapienza, CNR, Inst Mol Biol & Pathol, I-00185 Rome, Italy.;Univ Roma La Sapienza, Dept Biochem Sci, I-00185 Rome, Italy..
Univ Roma La Sapienza, CNR, Inst Mol Biol & Pathol, I-00185 Rome, Italy.;Univ Roma La Sapienza, Dept Biochem Sci, I-00185 Rome, Italy..
Univ Autonoma Madrid, CSIC, Ctr Biol Mol Severo Ochoa, Dept Biol Celular & Inmunol, Canto Blanco, Spain.;Ctr Invest Biomed Red Enfermedades Hepat & Digest, Madrid, Spain..
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2015 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 5, 16828Article in journal (Refereed) Published
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Abstract [en]

Sorcin is an essential penta-EF hand calcium binding protein, able to confer the multi-drug resistance phenotype to drug-sensitive cancer cells and to reduce Endoplasmic Reticulum stress and cell death. Sorcin silencing blocks cell cycle progression in mitosis and induces cell death by triggering apoptosis. Sorcin participates in the modulation of calcium homeostasis and in calcium-dependent cell signalling in normal and cancer cells. The molecular basis of Sorcin action is yet unknown. The X-ray structures of Sorcin in the apo (apoSor) and in calcium bound form (CaSor) reveal the structural basis of Sorcin action: calcium binding to the EF1-3 hands promotes a large conformational change, involving a movement of the long D-helix joining the EF1-EF2 sub-domain to EF3 and the opening of EF1. This movement promotes the exposure of a hydrophobic pocket, which can accommodate in CaSor the portion of its N-terminal domain displaying the consensus binding motif identified by phage display experiments. This domain inhibits the interaction of sorcin with PDCD6, a protein that carries the Sorcin consensus motif, co-localizes with Sorcin in the perinuclear region of the cell and in the midbody and is involved in the onset of apoptosis.

Place, publisher, year, edition, pages
2015. Vol. 5, 16828
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Medicinal Chemistry
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URN: urn:nbn:se:uu:diva-270106OAI: oai:DiVA.org:uu-270106DiVA: diva2:885896
Funder
Swedish Research CouncilĂ…ke Wiberg Foundation
Available from: 2015-12-21 Created: 2015-12-21 Last updated: 2017-12-01

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Sundell, Gustav N.Ivarsson, Ylva

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