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LC3 and Autophagy | SpringerLink
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Microtubule-associated protein 1A/1B-light chain 3 (LC3) is a soluble protein with a molecular mass of ∼17 kDa that is distributed ubiquitously in mammalian tissues and cultured cells. During autophagy, autophagosomes engulf cytoplasmic components,...
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leupeptin-administered rat liver springer science+business media human apg3p/aut1p homologue describe basic protocols including cytosolic proteins privacy choices/manage cookies form lc3-phosphatidylethanolamine conjugate intra-autophagosomal components microtubule binding subunit protein-activating enzyme late autophagic vacuoles humana press authentic e2 enzyme autophagosomal membrane depending form-ii formation journal finder publish european economic area nervous system diseases host defence mechanism saccharomyces cerevisiae apg7p endoplasmic reticulum preserved betaine homocysteine methyltransferase limited degradation fragment inhibiting tyrosine hydroxylase endogenous lc3-ii conditions privacy policy phagosome isei tanida mammalian atg8 modifiers mycobacterium tuberculosis inhibition lc3-positive structures autophagy-related processes autophagy generate sites accepting optional cookies juntendo university school main content log lc3 conjugation system light chain 3 multiple substrates autophagosomal membranes autophagic vacuoles check access ethics access journal publish mammalian cells lc3-ii cytosolic form chapter log protocol tanida monitoring autophagy privacy policy
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ScholarlyArticle:
headline:LC3 and Autophagy
pageEnd:88
pageStart:77
image:https://media.springernature.com/w153/springer-static/cover/book/978-1-59745-157-4.jpg
genre:
Springer Protocols
isPartOf:
name:Autophagosome and Phagosome
isbn:
978-1-59745-157-4
978-1-58829-853-9
type:Book
publisher:
name:Humana Press
logo:
url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
type:ImageObject
type:Organization
author:
name:Isei Tanida
affiliation:
name:Juntendo University School of Medicine
address:
name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
type:PostalAddress
type:Organization
type:Person
name:Takashi Ueno
affiliation:
name:Juntendo University School of Medicine
address:
name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
type:PostalAddress
type:Organization
type:Person
name:Eiki Kominami
affiliation:
name:Juntendo University School of Medicine
address:
name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
type:PostalAddress
type:Organization
type:Person
keywords:LC3, lipidation, ubiquitylation-like reaction, autophagosome, autolysosome, autophagy,
ATG conjugation system
description:Microtubule-associated protein 1A/1B-light chain 3 (LC3) is a soluble protein with a molecular mass of βΌ17βkDa that is distributed ubiquitously in mammalian tissues and cultured cells. During autophagy, autophagosomes engulf cytoplasmic components, including cytosolic proteins and organelles. Concomitantly, a cytosolic form of LC3 (LC3-I) is conjugated to phosphatidylethanolamine to form LC3-phosphatidylethanolamine conjugate (LC3-II), which is recruited to autophagosomal membranes. Autophagosomes fuse with lysosomes to form autolysosomes, and intra-autophagosomal components are degraded by lysosomal hydrolases. At the same time, LC3-II in autolysosomal lumen is degraded. Thus, lysosomal turnover of the autophagosomal marker LC3-II reflects starvation-induced autophagic activity, and detecting LC3 by immunoblotting or immunofluorescence has become a reliable method for monitoring autophagy and autophagy-related processes, including autophagic cell death. Here we describe basic protocols to assay for endogenous LC3-II by immunoblotting, immunoprecipitation, and immunofluorescence.
datePublished:2008
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978-1-59745-157-4
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name:Juntendo University School of Medicine
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name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
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name:Takashi Ueno
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