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MERIT, a cellular system coordinating lysosomal repair, removal and replacement.

Identifieur interne : 000092 ( Main/Exploration ); précédent : 000091; suivant : 000093

MERIT, a cellular system coordinating lysosomal repair, removal and replacement.

Auteurs : Jingyue Jia [États-Unis] ; Aurore Claude-Taupin [États-Unis] ; Yuexi Gu [États-Unis] ; Seong Won Choi [États-Unis] ; Ryan Peters [États-Unis] ; Bhawana Bissa [États-Unis] ; Michal H. Mudd [États-Unis] ; Lee Allers [États-Unis] ; Sandeep Pallikkuth [États-Unis] ; Keith A. Lidke [États-Unis] ; Michelle Salemi [États-Unis] ; Brett Phinney [États-Unis] ; Muriel Mari [Pays-Bas] ; Fulvio Reggiori [Pays-Bas] ; Vojo Deretic [États-Unis]

Source :

RBID : pubmed:32521192

Abstract

Membrane integrity is essential for cellular survival and function. The spectrum of mechanisms protecting cellular and intracellular membranes is not fully known. Our recent work has uncovered a cellular system termed MERIT for lysosomal membrane repair, removal and replacement. Specifically, lysosomal membrane damage induces, in succession, ESCRT-dependent membrane repair, macroautophagy/autophagy-dominant removal of damaged lysosomes, and initiation of lysosomal biogenesis via transcriptional programs. The MERIT system is governed by galectins, a family of cytosolically synthesized lectins recognizing β-galactoside glycans. We found in this study that LGALS3 (galectin 3) detects membrane damage by detecting exposed lumenal glycosyl groups, recruits and organizes ESCRT components PDCD6IP/ALIX, CHMP4A, and CHMPB at damaged sites on the lysosomes, and facilitates ESCRT-driven repair of lysosomal membrane. At later stages, LGALS3 cooperates with TRIM16, an autophagy receptor-regulator, to engage autophagy machinery in removal of excessively damaged lysosomes. In the absence of LGALS3, repair and autophagy are less efficient, whereas TFEB nuclear translocation increases to compensate lysosomal deficiency via de novo lysosomal biogenesis. The MERIT system protects endomembrane integrity against a broad spectrum of agents damaging the endolysosomal network including lysosomotropic drugs, Mycobacterium tuberculosis, or neurotoxic MAPT/tau.

ABBREVIATIONS

AMPK: AMP-activated protein kinase; APEX2: engineered ascorbate peroxidase 2; ATG13: autophagy related 13; ATG16L1: autophagy related 16 like 1; BMMs: bone marrow-derived macrophages; ESCRT: endosomal sorting complexes required for transport; GPN: glycyl-L-phenylalanine 2-naphthylamide; LLOMe: L-leucyl-L-leucine methyl ester; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MERIT: membrane repair, removal and replacement; MTOR: mechanistic target of rapamycin kinase; TFEB: transcription factor EB; TFRC: transferrin receptor; TRIM16: tripartite motif-containing 16.


DOI: 10.1080/15548627.2020.1779451
PubMed: 32521192
PubMed Central: PMC7469593


Affiliations:


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<div type="abstract" xml:lang="en">Membrane integrity is essential for cellular survival and function. The spectrum of mechanisms protecting cellular and intracellular membranes is not fully known. Our recent work has uncovered a cellular system termed MERIT for lysosomal
<i>me</i>
mbrane
<i>re</i>
pa
<i>i</i>
r, removal and replacemen
<i>t</i>
. Specifically, lysosomal membrane damage induces, in succession, ESCRT-dependent membrane repair, macroautophagy/autophagy-dominant removal of damaged lysosomes, and initiation of lysosomal biogenesis via transcriptional programs. The MERIT system is governed by galectins, a family of cytosolically synthesized lectins recognizing β-galactoside glycans. We found in this study that LGALS3 (galectin 3) detects membrane damage by detecting exposed lumenal glycosyl groups, recruits and organizes ESCRT components PDCD6IP/ALIX, CHMP4A, and CHMPB at damaged sites on the lysosomes, and facilitates ESCRT-driven repair of lysosomal membrane. At later stages, LGALS3 cooperates with TRIM16, an autophagy receptor-regulator, to engage autophagy machinery in removal of excessively damaged lysosomes. In the absence of LGALS3, repair and autophagy are less efficient, whereas TFEB nuclear translocation increases to compensate lysosomal deficiency via de novo lysosomal biogenesis. The MERIT system protects endomembrane integrity against a broad spectrum of agents damaging the endolysosomal network including lysosomotropic drugs,
<i>Mycobacterium tuberculosis</i>
, or neurotoxic MAPT/tau.</div>
<div type="abstract" xml:lang="en">
<p>
<b>ABBREVIATIONS</b>
</p>
<p>AMPK: AMP-activated protein kinase; APEX2: engineered ascorbate peroxidase 2; ATG13: autophagy related 13; ATG16L1: autophagy related 16 like 1; BMMs: bone marrow-derived macrophages; ESCRT: endosomal sorting complexes required for transport; GPN: glycyl-L-phenylalanine 2-naphthylamide; LLOMe: L-leucyl-L-leucine methyl ester; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MERIT: membrane repair, removal and replacement; MTOR: mechanistic target of rapamycin kinase; TFEB: transcription factor EB; TFRC: transferrin receptor; TRIM16: tripartite motif-containing 16.</p>
</div>
</front>
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<Day>29</Day>
</DateRevised>
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<Volume>16</Volume>
<Issue>8</Issue>
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<Month>08</Month>
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<Title>Autophagy</Title>
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<ArticleTitle>MERIT, a cellular system coordinating lysosomal repair, removal and replacement.</ArticleTitle>
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<AbstractText>Membrane integrity is essential for cellular survival and function. The spectrum of mechanisms protecting cellular and intracellular membranes is not fully known. Our recent work has uncovered a cellular system termed MERIT for lysosomal
<i>me</i>
mbrane
<i>re</i>
pa
<i>i</i>
r, removal and replacemen
<i>t</i>
. Specifically, lysosomal membrane damage induces, in succession, ESCRT-dependent membrane repair, macroautophagy/autophagy-dominant removal of damaged lysosomes, and initiation of lysosomal biogenesis via transcriptional programs. The MERIT system is governed by galectins, a family of cytosolically synthesized lectins recognizing β-galactoside glycans. We found in this study that LGALS3 (galectin 3) detects membrane damage by detecting exposed lumenal glycosyl groups, recruits and organizes ESCRT components PDCD6IP/ALIX, CHMP4A, and CHMPB at damaged sites on the lysosomes, and facilitates ESCRT-driven repair of lysosomal membrane. At later stages, LGALS3 cooperates with TRIM16, an autophagy receptor-regulator, to engage autophagy machinery in removal of excessively damaged lysosomes. In the absence of LGALS3, repair and autophagy are less efficient, whereas TFEB nuclear translocation increases to compensate lysosomal deficiency via de novo lysosomal biogenesis. The MERIT system protects endomembrane integrity against a broad spectrum of agents damaging the endolysosomal network including lysosomotropic drugs,
<i>Mycobacterium tuberculosis</i>
, or neurotoxic MAPT/tau.</AbstractText>
<AbstractText Label="ABBREVIATIONS">AMPK: AMP-activated protein kinase; APEX2: engineered ascorbate peroxidase 2; ATG13: autophagy related 13; ATG16L1: autophagy related 16 like 1; BMMs: bone marrow-derived macrophages; ESCRT: endosomal sorting complexes required for transport; GPN: glycyl-L-phenylalanine 2-naphthylamide; LLOMe: L-leucyl-L-leucine methyl ester; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MERIT: membrane repair, removal and replacement; MTOR: mechanistic target of rapamycin kinase; TFEB: transcription factor EB; TFRC: transferrin receptor; TRIM16: tripartite motif-containing 16.</AbstractText>
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<LastName>Salemi</LastName>
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<name sortKey="Phinney, Brett" sort="Phinney, Brett" uniqKey="Phinney B" first="Brett" last="Phinney">Brett Phinney</name>
<name sortKey="Salemi, Michelle" sort="Salemi, Michelle" uniqKey="Salemi M" first="Michelle" last="Salemi">Michelle Salemi</name>
</country>
<country name="Pays-Bas">
<region name="Groningue (province)">
<name sortKey="Mari, Muriel" sort="Mari, Muriel" uniqKey="Mari M" first="Muriel" last="Mari">Muriel Mari</name>
</region>
<name sortKey="Reggiori, Fulvio" sort="Reggiori, Fulvio" uniqKey="Reggiori F" first="Fulvio" last="Reggiori">Fulvio Reggiori</name>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Bois/explor/RapamycinFungusV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000092 | SxmlIndent | more

Ou

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000092 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Bois
   |area=    RapamycinFungusV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:32521192
   |texte=   MERIT, a cellular system coordinating lysosomal repair, removal and replacement.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:32521192" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a RapamycinFungusV1 

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This area was generated with Dilib version V0.6.38.
Data generation: Thu Nov 19 21:55:41 2020. Site generation: Thu Nov 19 22:00:39 2020