Cargando…

WIPI-dependent autophagy during neutrophil differentiation of NB4 acute promyelocytic leukemia cells

Members of the WD-repeat protein interacting with phosphoinositides (WIPI) family are phosphatidylinositol 3-phosphate (PI3P) effectors that are essential for the formation of autophagosomes. Autophagosomes, unique double-membraned organelles, are characteristic for autophagy, a bulk degradation mec...

Descripción completa

Detalles Bibliográficos
Autores principales: Brigger, D, Proikas-Cezanne, T, Tschan, M P
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4123064/
https://www.ncbi.nlm.nih.gov/pubmed/24991767
http://dx.doi.org/10.1038/cddis.2014.261
_version_ 1782329449121841152
author Brigger, D
Proikas-Cezanne, T
Tschan, M P
author_facet Brigger, D
Proikas-Cezanne, T
Tschan, M P
author_sort Brigger, D
collection PubMed
description Members of the WD-repeat protein interacting with phosphoinositides (WIPI) family are phosphatidylinositol 3-phosphate (PI3P) effectors that are essential for the formation of autophagosomes. Autophagosomes, unique double-membraned organelles, are characteristic for autophagy, a bulk degradation mechanism with cytoprotective and homeostatic function. Both, WIPI-1 and WIPI-2 are aberrantly expressed in several solid tumors, linking these genes to carcinogenesis. We now found that the expression of WIPI-1 was significantly reduced in a large cohort of 98 primary acute myeloid leukemia (AML) patient samples (complex karyotypes; t(8;21); t(15,17); inv(16)). In contrast, the expression of WIPI-2 was only reduced in acute promyelocytic leukemia (APL), a distinct subtype of AML (t(15,17)). As AML cells are blocked in their differentiation, we tested if the expression levels of WIPI-1 and WIPI-2 increase during all-trans retinoic acid (ATRA)-induced neutrophil differentiation of APL. According to the higher WIPI-1 expression in granulocytes compared with immature blast cells, WIPI-1 but not WIPI-2 expression was significantly induced during neutrophil differentiation of NB4 APL cells. Interestingly, the induction of WIPI-1 expression was dependent on the transcription factor PU.1, a master regulator of myelopoiesis, supporting our notion that WIPI-1 expression is reduced in AML patients lacking proper PU-1 activity. Further, knocking down WIPI-1 in NB4 cells markedly attenuated the autophagic flux and significantly reduced neutrophil differentiation. This result was also achieved by knocking down WIPI-2, suggesting that both WIPI-1 and WIPI-2 are functionally required and not redundant in mediating the PI3P signal at the onset of autophagy in NB4 cells. In line with these data, downregulation of PI3KC3 (hVPS34), which generates PI3P upstream of WIPIs, also inhibited neutrophil differentiation. In conclusion, we demonstrate that both WIPI-1 and WIPI-2 are required for the PI3P-dependent autophagic activity during neutrophil differentiation, and that PU.1-dependent WIPI-1 expression is significantly repressed in primary AML patient samples and that the induction of autophagic flux is associated with neutrophil differentiation of APL cells.
format Online
Article
Text
id pubmed-4123064
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher Nature Publishing Group
record_format MEDLINE/PubMed
spelling pubmed-41230642014-08-15 WIPI-dependent autophagy during neutrophil differentiation of NB4 acute promyelocytic leukemia cells Brigger, D Proikas-Cezanne, T Tschan, M P Cell Death Dis Original Article Members of the WD-repeat protein interacting with phosphoinositides (WIPI) family are phosphatidylinositol 3-phosphate (PI3P) effectors that are essential for the formation of autophagosomes. Autophagosomes, unique double-membraned organelles, are characteristic for autophagy, a bulk degradation mechanism with cytoprotective and homeostatic function. Both, WIPI-1 and WIPI-2 are aberrantly expressed in several solid tumors, linking these genes to carcinogenesis. We now found that the expression of WIPI-1 was significantly reduced in a large cohort of 98 primary acute myeloid leukemia (AML) patient samples (complex karyotypes; t(8;21); t(15,17); inv(16)). In contrast, the expression of WIPI-2 was only reduced in acute promyelocytic leukemia (APL), a distinct subtype of AML (t(15,17)). As AML cells are blocked in their differentiation, we tested if the expression levels of WIPI-1 and WIPI-2 increase during all-trans retinoic acid (ATRA)-induced neutrophil differentiation of APL. According to the higher WIPI-1 expression in granulocytes compared with immature blast cells, WIPI-1 but not WIPI-2 expression was significantly induced during neutrophil differentiation of NB4 APL cells. Interestingly, the induction of WIPI-1 expression was dependent on the transcription factor PU.1, a master regulator of myelopoiesis, supporting our notion that WIPI-1 expression is reduced in AML patients lacking proper PU-1 activity. Further, knocking down WIPI-1 in NB4 cells markedly attenuated the autophagic flux and significantly reduced neutrophil differentiation. This result was also achieved by knocking down WIPI-2, suggesting that both WIPI-1 and WIPI-2 are functionally required and not redundant in mediating the PI3P signal at the onset of autophagy in NB4 cells. In line with these data, downregulation of PI3KC3 (hVPS34), which generates PI3P upstream of WIPIs, also inhibited neutrophil differentiation. In conclusion, we demonstrate that both WIPI-1 and WIPI-2 are required for the PI3P-dependent autophagic activity during neutrophil differentiation, and that PU.1-dependent WIPI-1 expression is significantly repressed in primary AML patient samples and that the induction of autophagic flux is associated with neutrophil differentiation of APL cells. Nature Publishing Group 2014-07 2014-07-03 /pmc/articles/PMC4123064/ /pubmed/24991767 http://dx.doi.org/10.1038/cddis.2014.261 Text en Copyright © 2014 Macmillan Publishers Limited http://creativecommons.org/licenses/by-nc-sa/3.0/ Cell Death and Disease is an open-access journal published by Nature Publishing Group. This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/
spellingShingle Original Article
Brigger, D
Proikas-Cezanne, T
Tschan, M P
WIPI-dependent autophagy during neutrophil differentiation of NB4 acute promyelocytic leukemia cells
title WIPI-dependent autophagy during neutrophil differentiation of NB4 acute promyelocytic leukemia cells
title_full WIPI-dependent autophagy during neutrophil differentiation of NB4 acute promyelocytic leukemia cells
title_fullStr WIPI-dependent autophagy during neutrophil differentiation of NB4 acute promyelocytic leukemia cells
title_full_unstemmed WIPI-dependent autophagy during neutrophil differentiation of NB4 acute promyelocytic leukemia cells
title_short WIPI-dependent autophagy during neutrophil differentiation of NB4 acute promyelocytic leukemia cells
title_sort wipi-dependent autophagy during neutrophil differentiation of nb4 acute promyelocytic leukemia cells
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4123064/
https://www.ncbi.nlm.nih.gov/pubmed/24991767
http://dx.doi.org/10.1038/cddis.2014.261
work_keys_str_mv AT briggerd wipidependentautophagyduringneutrophildifferentiationofnb4acutepromyelocyticleukemiacells
AT proikascezannet wipidependentautophagyduringneutrophildifferentiationofnb4acutepromyelocyticleukemiacells
AT tschanmp wipidependentautophagyduringneutrophildifferentiationofnb4acutepromyelocyticleukemiacells