Chasing the elusive mammalian microautophagy

Laura Santambrogio, Ana Maria Cuervo

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

Different mechanisms for delivery of intracellular components (proteins and organelles) to lysosomes and late endosomes for degradation co-exist in almost all cells and set the basis for distinct autophagic pathways. Cargo can be sequestered inside double-membrane vesicles (or autophagosomes) and reach the lysosomal compartment upon fusion of these vesicles to lysosomes through macroautophagy. In a different type of autophagy, known as chaperone-mediated autophagy (CMA), single individual soluble proteins can be targeted one by one to the lysosomal membrane and translocated into the lumen for degradation. Direct sequestration of proteins and organelles by invaginations at the lysosomal membrane that pinch off into the lumen has also been proposed. This process, known as microautophagy, remains poorly understood in mammalian cells. In our recent work, we demonstrate the occurrence of both "in bulk" and "selective" internalization of cytosolic components in late endosomes and identify some of the molecular players of this process that we have named endosomalmicroautophagy (e-MI) due to its resemblance to microautophagy.

Original languageEnglish (US)
Pages (from-to)652-654
Number of pages3
JournalAutophagy
Volume7
Issue number6
DOIs
StatePublished - Jun 2011

Fingerprint

Autophagy
Endosomes
Lysosomes
Organelles
Membranes
Proteins

Keywords

  • ESCRT proteins
  • hsc70
  • Late endosomes
  • Multivesicular bodies

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

Chasing the elusive mammalian microautophagy. / Santambrogio, Laura; Cuervo, Ana Maria.

In: Autophagy, Vol. 7, No. 6, 06.2011, p. 652-654.

Research output: Contribution to journalArticle

Santambrogio, Laura ; Cuervo, Ana Maria. / Chasing the elusive mammalian microautophagy. In: Autophagy. 2011 ; Vol. 7, No. 6. pp. 652-654.
@article{dc946f33415f4e4094fab86fcfd34482,
title = "Chasing the elusive mammalian microautophagy",
abstract = "Different mechanisms for delivery of intracellular components (proteins and organelles) to lysosomes and late endosomes for degradation co-exist in almost all cells and set the basis for distinct autophagic pathways. Cargo can be sequestered inside double-membrane vesicles (or autophagosomes) and reach the lysosomal compartment upon fusion of these vesicles to lysosomes through macroautophagy. In a different type of autophagy, known as chaperone-mediated autophagy (CMA), single individual soluble proteins can be targeted one by one to the lysosomal membrane and translocated into the lumen for degradation. Direct sequestration of proteins and organelles by invaginations at the lysosomal membrane that pinch off into the lumen has also been proposed. This process, known as microautophagy, remains poorly understood in mammalian cells. In our recent work, we demonstrate the occurrence of both {"}in bulk{"} and {"}selective{"} internalization of cytosolic components in late endosomes and identify some of the molecular players of this process that we have named endosomalmicroautophagy (e-MI) due to its resemblance to microautophagy.",
keywords = "ESCRT proteins, hsc70, Late endosomes, Multivesicular bodies",
author = "Laura Santambrogio and Cuervo, {Ana Maria}",
year = "2011",
month = "6",
doi = "10.4161/auto.7.6.15287",
language = "English (US)",
volume = "7",
pages = "652--654",
journal = "Autophagy",
issn = "1554-8627",
publisher = "Landes Bioscience",
number = "6",

}

TY - JOUR

T1 - Chasing the elusive mammalian microautophagy

AU - Santambrogio, Laura

AU - Cuervo, Ana Maria

PY - 2011/6

Y1 - 2011/6

N2 - Different mechanisms for delivery of intracellular components (proteins and organelles) to lysosomes and late endosomes for degradation co-exist in almost all cells and set the basis for distinct autophagic pathways. Cargo can be sequestered inside double-membrane vesicles (or autophagosomes) and reach the lysosomal compartment upon fusion of these vesicles to lysosomes through macroautophagy. In a different type of autophagy, known as chaperone-mediated autophagy (CMA), single individual soluble proteins can be targeted one by one to the lysosomal membrane and translocated into the lumen for degradation. Direct sequestration of proteins and organelles by invaginations at the lysosomal membrane that pinch off into the lumen has also been proposed. This process, known as microautophagy, remains poorly understood in mammalian cells. In our recent work, we demonstrate the occurrence of both "in bulk" and "selective" internalization of cytosolic components in late endosomes and identify some of the molecular players of this process that we have named endosomalmicroautophagy (e-MI) due to its resemblance to microautophagy.

AB - Different mechanisms for delivery of intracellular components (proteins and organelles) to lysosomes and late endosomes for degradation co-exist in almost all cells and set the basis for distinct autophagic pathways. Cargo can be sequestered inside double-membrane vesicles (or autophagosomes) and reach the lysosomal compartment upon fusion of these vesicles to lysosomes through macroautophagy. In a different type of autophagy, known as chaperone-mediated autophagy (CMA), single individual soluble proteins can be targeted one by one to the lysosomal membrane and translocated into the lumen for degradation. Direct sequestration of proteins and organelles by invaginations at the lysosomal membrane that pinch off into the lumen has also been proposed. This process, known as microautophagy, remains poorly understood in mammalian cells. In our recent work, we demonstrate the occurrence of both "in bulk" and "selective" internalization of cytosolic components in late endosomes and identify some of the molecular players of this process that we have named endosomalmicroautophagy (e-MI) due to its resemblance to microautophagy.

KW - ESCRT proteins

KW - hsc70

KW - Late endosomes

KW - Multivesicular bodies

UR - http://www.scopus.com/inward/record.url?scp=79957881200&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79957881200&partnerID=8YFLogxK

U2 - 10.4161/auto.7.6.15287

DO - 10.4161/auto.7.6.15287

M3 - Article

C2 - 21460618

AN - SCOPUS:79957881200

VL - 7

SP - 652

EP - 654

JO - Autophagy

JF - Autophagy

SN - 1554-8627

IS - 6

ER -