LC3/GABARAP family proteins: autophagy‐(un)related functions. Issue 12 (6th September 2016)
- Record Type:
- Journal Article
- Title:
- LC3/GABARAP family proteins: autophagy‐(un)related functions. Issue 12 (6th September 2016)
- Main Title:
- LC3/GABARAP family proteins: autophagy‐(un)related functions
- Authors:
- Schaaf, Marco B. E.
Keulers, Tom G.
Vooijs, Marc A.
Rouschop, Kasper M. A. - Abstract:
- ABSTRACT: From yeast to mammals, autophagy is an important mechanism for sustaining cellular homeostasis through facilitating the degradation and recycling of aged and cytotoxic components. During autophagy, cargo is captured in double‐membraned vesicles, the autophagosomes, and degraded through lysosomal fusion. In yeast, autophagy initiation, cargo recognition, cargo engulfment, and vesicle closure is Atg8 dependent. In higher eukaryotes, Atg8 has evolved into the LC3/GABARAP protein family, consisting of 7 family proteins [LC3A(2 splice variants), LC3B, LC3C, GABARAP, GABARAPL1, and GABARAPL2]. LC3B, the most studied family protein, is associatedwith autophagosome development and maturation and is used tomonitor autophagic activity. Giventhe high homology, the other LC3/GABARAP family proteins are often presumed to fulfill similar functions. Nevertheless, substantial evidence shows that the LC3/GABARAP family proteins are unique in function and important in autophagy‐independent mechanisms. In this review, we discuss the current knowledge and functions of the LC3/GABARAP family proteins. We focus on processing of the individual family proteins and their role in autophagy initiation, cargo recognition, vesicle closure, and trafficking, a complex and tightly regulated process that requires selective presentation and recruitment of these family proteins. In addition, functions unrelated to autophagy of the LC3/GABARAP protein family members are discussed.—Schaaf, M. B. E.,ABSTRACT: From yeast to mammals, autophagy is an important mechanism for sustaining cellular homeostasis through facilitating the degradation and recycling of aged and cytotoxic components. During autophagy, cargo is captured in double‐membraned vesicles, the autophagosomes, and degraded through lysosomal fusion. In yeast, autophagy initiation, cargo recognition, cargo engulfment, and vesicle closure is Atg8 dependent. In higher eukaryotes, Atg8 has evolved into the LC3/GABARAP protein family, consisting of 7 family proteins [LC3A(2 splice variants), LC3B, LC3C, GABARAP, GABARAPL1, and GABARAPL2]. LC3B, the most studied family protein, is associatedwith autophagosome development and maturation and is used tomonitor autophagic activity. Giventhe high homology, the other LC3/GABARAP family proteins are often presumed to fulfill similar functions. Nevertheless, substantial evidence shows that the LC3/GABARAP family proteins are unique in function and important in autophagy‐independent mechanisms. In this review, we discuss the current knowledge and functions of the LC3/GABARAP family proteins. We focus on processing of the individual family proteins and their role in autophagy initiation, cargo recognition, vesicle closure, and trafficking, a complex and tightly regulated process that requires selective presentation and recruitment of these family proteins. In addition, functions unrelated to autophagy of the LC3/GABARAP protein family members are discussed.—Schaaf, M. B. E., Keulers, T. G, Vooijs, M. A., Rouschop, K. M. A. LC3/GABARAP family proteins: autophagy‐(un)related functions. FASEB J. 30, 3961–3978 (2016). www.fasebj.org … (more)
- Is Part Of:
- FASEB journal. Volume 30:Issue 12(2016)
- Journal:
- FASEB journal
- Issue:
- Volume 30:Issue 12(2016)
- Issue Display:
- Volume 30, Issue 12 (2016)
- Year:
- 2016
- Volume:
- 30
- Issue:
- 12
- Issue Sort Value:
- 2016-0030-0012-0000
- Page Start:
- 3961
- Page End:
- 3978
- Publication Date:
- 2016-09-06
- Subjects:
- cancer -- ATG7 -- Atg8 orthologues -- autophagosome
Biology -- Periodicals
Biology, Experimental -- Periodicals
570 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1096/fj.201600698R ↗
- Languages:
- English
- ISSNs:
- 0892-6638
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 13229.xml