PML regulates apoptosis at endoplasmic reticulum by modulating calcium release
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-associa...
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| Published in: | Science (American Association for the Advancement of Science) Vol. 330; no. 6008; p. 1247 |
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| Main Authors: | , , , , , , , , , , , , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
United States
26.11.2010
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| Subjects: | |
| ISSN: | 1095-9203, 1095-9203 |
| Online Access: | Get more information |
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| Abstract | 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. |
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| AbstractList | 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. 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.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. |
| Author | Lin, Hui-Kuan Giorgi, Carlotta Tacchetti, Carlo Bernardi, Rosa Pinton, Paolo Duszynski, Jerzy Ito, Keisuke Lebiedzinska, Magdalena Pandolfi, Pier Paolo Bonora, Massimo Rizzuto, Rosario Santangelo, Clara Wieckowski, Mariusz R Bononi, Angela |
| Author_xml | – sequence: 1 givenname: Carlotta surname: Giorgi fullname: Giorgi, Carlotta organization: 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 – sequence: 2 givenname: Keisuke surname: Ito fullname: Ito, Keisuke – sequence: 3 givenname: Hui-Kuan surname: Lin fullname: Lin, Hui-Kuan – sequence: 4 givenname: Clara surname: Santangelo fullname: Santangelo, Clara – sequence: 5 givenname: Mariusz R surname: Wieckowski fullname: Wieckowski, Mariusz R – sequence: 6 givenname: Magdalena surname: Lebiedzinska fullname: Lebiedzinska, Magdalena – sequence: 7 givenname: Angela surname: Bononi fullname: Bononi, Angela – sequence: 8 givenname: Massimo surname: Bonora fullname: Bonora, Massimo – sequence: 9 givenname: Jerzy surname: Duszynski fullname: Duszynski, Jerzy – sequence: 10 givenname: Rosa surname: Bernardi fullname: Bernardi, Rosa – sequence: 11 givenname: Rosario surname: Rizzuto fullname: Rizzuto, Rosario – sequence: 12 givenname: Carlo surname: Tacchetti fullname: Tacchetti, Carlo – sequence: 13 givenname: Paolo surname: Pinton fullname: Pinton, Paolo – sequence: 14 givenname: Pier Paolo surname: Pandolfi fullname: Pandolfi, Pier Paolo |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21030605$$D View this record in MEDLINE/PubMed |
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| References | 21109655 - Science. 2010 Nov 26;330(6008):1183-4. doi: 10.1126/science.1199405. 21145493 - Dev Cell. 2010 Dec 14;19(6):789-90. doi: 10.1016/j.devcel.2010.11.013. 33766887 - Science. 2021 Mar 26;371(6536):eabi4740. doi: 10.1126/science.abi4740. |
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| Snippet | The promyelocytic leukemia (PML) tumor suppressor is a pleiotropic modulator of apoptosis. However, the molecular basis for such a diverse proapoptotic role is... |
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| SubjectTerms | 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 Nuclear Proteins - metabolism Phosphorylation Promyelocytic Leukemia Protein Protein Phosphatase 2 - metabolism Proto-Oncogene Proteins c-akt - metabolism Recombinant Fusion Proteins - metabolism Stress, Physiological Transcription Factors - genetics Transcription Factors - metabolism Tumor Suppressor Proteins - genetics Tumor Suppressor Proteins - metabolism |
| Title | PML regulates apoptosis at endoplasmic reticulum by modulating calcium release |
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