Document Detail


PML regulates apoptosis at endoplasmic reticulum by modulating calcium release.
MedLine Citation:
PMID:  21030605     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The promyelocytic leukemia (PML) tumor suppressor is a pleiotropic modulator of apoptosis. However, the molecular basis for such a diverse proapoptotic role is currently unknown. We show that extranuclear Pml was specifically enriched at the endoplasmic reticulum (ER) and at the mitochondria-associated membranes, signaling domains involved in ER-to-mitochondria calcium ion (Ca(2+)) transport and in induction of apoptosis. We found Pml in complexes of large molecular size with the inositol 1,4,5-trisphosphate receptor (IP(3)R), protein kinase Akt, and protein phosphatase 2a (PP2a). Pml was essential for Akt- and PP2a-dependent modulation of IP(3)R phosphorylation and in turn for IP(3)R-mediated Ca(2+) release from ER. Our findings provide a mechanistic explanation for the pleiotropic role of Pml in apoptosis and identify a pharmacological target for the modulation of Ca(2+) signals.
Authors:
Carlotta Giorgi; Keisuke Ito; Hui-Kuan Lin; Clara Santangelo; Mariusz R Wieckowski; Magdalena Lebiedzinska; Angela Bononi; Massimo Bonora; Jerzy Duszynski; Rosa Bernardi; Rosario Rizzuto; Carlo Tacchetti; Paolo Pinton; Pier Paolo Pandolfi
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2010-10-28
Journal Detail:
Title:  Science (New York, N.Y.)     Volume:  330     ISSN:  1095-9203     ISO Abbreviation:  Science     Publication Date:  2010 Nov 
Date Detail:
Created Date:  2010-11-26     Completed Date:  2010-12-10     Revised Date:  2013-05-23    
Medline Journal Info:
Nlm Unique ID:  0404511     Medline TA:  Science     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1247-51     Citation Subset:  IM    
Affiliation:
Department of Experimental and Diagnostic Medicine, Section of General Pathology, Interdisciplinary Center for the Study of Inflammation (ICSI), Emilia Romagna Laboratory BioPharmaNet, and Laboratory for Technologies of Advanced Therapies (LTTA) University of Ferrara, Ferrara, Italy.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphate / metabolism
Animals
Apoptosis*
Calcium / metabolism*
Calcium Signaling*
Cell Line
Cell Nucleus / metabolism
Cells, Cultured
Cytosol / metabolism
Endoplasmic Reticulum / metabolism*
Homeostasis
Humans
Inositol 1,4,5-Trisphosphate / metabolism
Inositol 1,4,5-Trisphosphate Receptors / metabolism
Intracellular Membranes / metabolism
Mice
Mitochondria / metabolism
Nuclear Proteins / genetics,  metabolism*
Phosphorylation
Protein Phosphatase 2 / metabolism
Proto-Oncogene Proteins c-akt / metabolism
Recombinant Fusion Proteins / metabolism
Stress, Physiological
Transcription Factors / genetics,  metabolism*
Tumor Suppressor Proteins / genetics,  metabolism*
Grant Support
ID/Acronym/Agency:
GGP05284//Telethon; K99 CA139009/CA/NCI NIH HHS; K99 CA139009-01A1/CA/NCI NIH HHS; K99 CA139009-02/CA/NCI NIH HHS; R01 CA071692-04S1/CA/NCI NIH HHS; R01 CA102142-07/CA/NCI NIH HHS; R01 CA142874-01/CA/NCI NIH HHS; R01 CA142874-02/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Inositol 1,4,5-Trisphosphate Receptors; 0/Nuclear Proteins; 0/Pml protein, mouse; 0/Recombinant Fusion Proteins; 0/Transcription Factors; 0/Tumor Suppressor Proteins; 56-65-5/Adenosine Triphosphate; 7440-70-2/Calcium; 85166-31-0/Inositol 1,4,5-Trisphosphate; EC 2.7.11.1/Proto-Oncogene Proteins c-akt; EC 3.1.3.16/Protein Phosphatase 2
Comments/Corrections
Comment In:
Dev Cell. 2010 Dec 14;19(6):789-90   [PMID:  21145493 ]
Science. 2010 Nov 26;330(6008):1183-4   [PMID:  21109655 ]

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