S6K1 Is Indispensible for Stress-Induced Microtubule Acetylation and Autophagic Flux

Autophagy is a specific macromolecule and organelle degradation process. The target macromolecule or organelle is first enclosed in an autophagosome, and then delivered along acetylated microtubules to the lysosome. Autophagy is triggered by stress and largely contributes to cell survival. We have p...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Aleksandra Hać [verfasserIn] Karolina Pierzynowska [verfasserIn] Anna Herman-Antosiewicz [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2021

Schlagwörter:	S6 kinase 1 (S6K1) tubulin acetylation autophagic flux autophagosome-lysosome fusion serum deprivation sulforaphane

Übergeordnetes Werk:	In: Cells - MDPI AG, 2012, 10(2021), 4, p 929
Übergeordnetes Werk:	volume:10 ; year:2021 ; number:4, p 929

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/cells10040929

Katalog-ID:	DOAJ053642589

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allfieldsSound	10.3390/cells10040929 doi (DE-627)DOAJ053642589 (DE-599)DOAJ34128feae74744639b783557097b11c6 DE-627 ger DE-627 rakwb eng QH573-671 Aleksandra Hać verfasserin aut S6K1 Is Indispensible for Stress-Induced Microtubule Acetylation and Autophagic Flux 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Autophagy is a specific macromolecule and organelle degradation process. The target macromolecule or organelle is first enclosed in an autophagosome, and then delivered along acetylated microtubules to the lysosome. Autophagy is triggered by stress and largely contributes to cell survival. We have previously shown that S6K1 kinase is essential for autophagic flux under stress conditions. Here, we aimed to elucidate the underlying mechanism of S6K1 involvement in autophagy. We stimulated autophagy in S6K1/2 double-knockout mouse embryonic fibroblasts by exposing them to different stress conditions. Transient gene overexpression or silencing, immunoblotting, immunofluorescence, flow cytometry, and ratiometric fluorescence analyses revealed that the perturbation of autophagic flux in S6K1-deficient cells did not stem from impaired lysosomal function. Instead, the absence of S6K1 abolished stress-induced tubulin acetylation and disrupted the acetylated microtubule network, in turn impairing the autophagosome-lysosome fusion. S6K1 overexpression restored tubulin acetylation and autophagic flux in stressed S6K1/2-deficient cells. Similar effect of S6K1 status was observed in prostate cancer cells. Furthermore, overexpression of an acetylation-mimicking, but not acetylation-resistant, tubulin variant effectively restored autophagic flux in stressed S6K1/2-deficient cells. Collectively, S6K1 controls tubulin acetylation, hence contributing to the autophagic flux induced by different stress conditions and in different cells. S6 kinase 1 (S6K1) tubulin acetylation autophagic flux autophagosome-lysosome fusion serum deprivation sulforaphane Cytology Karolina Pierzynowska verfasserin aut Anna Herman-Antosiewicz verfasserin aut In Cells MDPI AG, 2012 10(2021), 4, p 929 (DE-627)718622081 (DE-600)2661518-6 20734409 nnns volume:10 year:2021 number:4, p 929 https://doi.org/10.3390/cells10040929 kostenfrei https://doaj.org/article/34128feae74744639b783557097b11c6 kostenfrei https://www.mdpi.com/2073-4409/10/4/929 kostenfrei https://doaj.org/toc/2073-4409 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2021 4, p 929
language	English
source	In Cells 10(2021), 4, p 929 volume:10 year:2021 number:4, p 929
sourceStr	In Cells 10(2021), 4, p 929 volume:10 year:2021 number:4, p 929
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topic_facet	S6 kinase 1 (S6K1) tubulin acetylation autophagic flux autophagosome-lysosome fusion serum deprivation sulforaphane Cytology
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container_title	Cells
authorswithroles_txt_mv	Aleksandra Hać @@aut@@ Karolina Pierzynowska @@aut@@ Anna Herman-Antosiewicz @@aut@@
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callnumber-first	Q - Science
author	Aleksandra Hać
spellingShingle	Aleksandra Hać misc QH573-671 misc S6 kinase 1 (S6K1) misc tubulin acetylation misc autophagic flux misc autophagosome-lysosome fusion misc serum deprivation misc sulforaphane misc Cytology S6K1 Is Indispensible for Stress-Induced Microtubule Acetylation and Autophagic Flux
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topic_title	QH573-671 S6K1 Is Indispensible for Stress-Induced Microtubule Acetylation and Autophagic Flux S6 kinase 1 (S6K1) tubulin acetylation autophagic flux autophagosome-lysosome fusion serum deprivation sulforaphane
topic	misc QH573-671 misc S6 kinase 1 (S6K1) misc tubulin acetylation misc autophagic flux misc autophagosome-lysosome fusion misc serum deprivation misc sulforaphane misc Cytology
topic_unstemmed	misc QH573-671 misc S6 kinase 1 (S6K1) misc tubulin acetylation misc autophagic flux misc autophagosome-lysosome fusion misc serum deprivation misc sulforaphane misc Cytology
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title	S6K1 Is Indispensible for Stress-Induced Microtubule Acetylation and Autophagic Flux
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title_full	S6K1 Is Indispensible for Stress-Induced Microtubule Acetylation and Autophagic Flux
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author_browse	Aleksandra Hać Karolina Pierzynowska Anna Herman-Antosiewicz
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title_sort	s6k1 is indispensible for stress-induced microtubule acetylation and autophagic flux
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title_auth	S6K1 Is Indispensible for Stress-Induced Microtubule Acetylation and Autophagic Flux
abstract	Autophagy is a specific macromolecule and organelle degradation process. The target macromolecule or organelle is first enclosed in an autophagosome, and then delivered along acetylated microtubules to the lysosome. Autophagy is triggered by stress and largely contributes to cell survival. We have previously shown that S6K1 kinase is essential for autophagic flux under stress conditions. Here, we aimed to elucidate the underlying mechanism of S6K1 involvement in autophagy. We stimulated autophagy in S6K1/2 double-knockout mouse embryonic fibroblasts by exposing them to different stress conditions. Transient gene overexpression or silencing, immunoblotting, immunofluorescence, flow cytometry, and ratiometric fluorescence analyses revealed that the perturbation of autophagic flux in S6K1-deficient cells did not stem from impaired lysosomal function. Instead, the absence of S6K1 abolished stress-induced tubulin acetylation and disrupted the acetylated microtubule network, in turn impairing the autophagosome-lysosome fusion. S6K1 overexpression restored tubulin acetylation and autophagic flux in stressed S6K1/2-deficient cells. Similar effect of S6K1 status was observed in prostate cancer cells. Furthermore, overexpression of an acetylation-mimicking, but not acetylation-resistant, tubulin variant effectively restored autophagic flux in stressed S6K1/2-deficient cells. Collectively, S6K1 controls tubulin acetylation, hence contributing to the autophagic flux induced by different stress conditions and in different cells.
abstractGer	Autophagy is a specific macromolecule and organelle degradation process. The target macromolecule or organelle is first enclosed in an autophagosome, and then delivered along acetylated microtubules to the lysosome. Autophagy is triggered by stress and largely contributes to cell survival. We have previously shown that S6K1 kinase is essential for autophagic flux under stress conditions. Here, we aimed to elucidate the underlying mechanism of S6K1 involvement in autophagy. We stimulated autophagy in S6K1/2 double-knockout mouse embryonic fibroblasts by exposing them to different stress conditions. Transient gene overexpression or silencing, immunoblotting, immunofluorescence, flow cytometry, and ratiometric fluorescence analyses revealed that the perturbation of autophagic flux in S6K1-deficient cells did not stem from impaired lysosomal function. Instead, the absence of S6K1 abolished stress-induced tubulin acetylation and disrupted the acetylated microtubule network, in turn impairing the autophagosome-lysosome fusion. S6K1 overexpression restored tubulin acetylation and autophagic flux in stressed S6K1/2-deficient cells. Similar effect of S6K1 status was observed in prostate cancer cells. Furthermore, overexpression of an acetylation-mimicking, but not acetylation-resistant, tubulin variant effectively restored autophagic flux in stressed S6K1/2-deficient cells. Collectively, S6K1 controls tubulin acetylation, hence contributing to the autophagic flux induced by different stress conditions and in different cells.
abstract_unstemmed	Autophagy is a specific macromolecule and organelle degradation process. The target macromolecule or organelle is first enclosed in an autophagosome, and then delivered along acetylated microtubules to the lysosome. Autophagy is triggered by stress and largely contributes to cell survival. We have previously shown that S6K1 kinase is essential for autophagic flux under stress conditions. Here, we aimed to elucidate the underlying mechanism of S6K1 involvement in autophagy. We stimulated autophagy in S6K1/2 double-knockout mouse embryonic fibroblasts by exposing them to different stress conditions. Transient gene overexpression or silencing, immunoblotting, immunofluorescence, flow cytometry, and ratiometric fluorescence analyses revealed that the perturbation of autophagic flux in S6K1-deficient cells did not stem from impaired lysosomal function. Instead, the absence of S6K1 abolished stress-induced tubulin acetylation and disrupted the acetylated microtubule network, in turn impairing the autophagosome-lysosome fusion. S6K1 overexpression restored tubulin acetylation and autophagic flux in stressed S6K1/2-deficient cells. Similar effect of S6K1 status was observed in prostate cancer cells. Furthermore, overexpression of an acetylation-mimicking, but not acetylation-resistant, tubulin variant effectively restored autophagic flux in stressed S6K1/2-deficient cells. Collectively, S6K1 controls tubulin acetylation, hence contributing to the autophagic flux induced by different stress conditions and in different cells.
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title_short	S6K1 Is Indispensible for Stress-Induced Microtubule Acetylation and Autophagic Flux
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author2	Karolina Pierzynowska Anna Herman-Antosiewicz
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S6K1 Is Indispensible for Stress-Induced Microtubule Acetylation and Autophagic Flux

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