PMID- 29233870
OWN - NLM
STAT- MEDLINE
DCOM- 20180122
LR  - 20181113
IS  - 1744-1358 (Electronic)
IS  - 0071-1365 (Print)
IS  - 0071-1365 (Linking)
VI  - 61
IP  - 6
DP  - 2017 Dec 12
TI  - The mammalian ULK1 complex and autophagy initiation.
PG  - 585-596
LID - 10.1042/EBC20170021 [doi]
AB  - Autophagy is a vital lysosomal degradation pathway that serves as a quality 
      control mechanism. It rids the cell of damaged, toxic or excess cellular 
      components, which if left to persist could be detrimental to the cell. It also 
      serves as a recycling pathway to maintain protein synthesis under starvation 
      conditions. A key initial event in autophagy is formation of the autophagosome, a 
      unique double-membrane organelle that engulfs the cytosolic cargo destined for 
      degradation. This step is mediated by the serine/threonine protein kinase ULK1 
      (unc-51-like kinase 1), which functions in a complex with at least three protein 
      partners: FIP200 (focal adhesion kinase family interacting protein of 200 kDa), 
      ATG (autophagy-related protein) 13 (ATG13), and ATG101. In this artcile, we focus 
      on the regulation of the ULK1 complex during autophagy initiation. The complex 
      pattern of upstream pathways that converge on ULK1 suggests that this complex 
      acts as a node, converting multiple signals into autophagosome formation. Here, 
      we review our current understanding of this regulation and in turn discuss what 
      happens downstream, once the ULK1 complex becomes activated.
CI  - (c) 2017 The Author(s).
FAU - Zachari, Maria
AU  - Zachari M
AD  - MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, 
      University of Dundee, Dundee DD1 5EH, U.K.
FAU - Ganley, Ian G
AU  - Ganley IG
AD  - MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, 
      University of Dundee, Dundee DD1 5EH, U.K. i.ganley@dundee.ac.uk.
LA  - eng
GR  - MC_UU_12016/4/Medical Research Council/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20171212
PL  - England
TA  - Essays Biochem
JT  - Essays in biochemistry
JID - 0043306
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Autophagy-Related Proteins)
RN  - 0 (Vesicular Transport Proteins)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.11.1 (Autophagy-Related Protein-1 Homolog)
SB  - IM
MH  - Adaptor Proteins, Signal Transducing/genetics/metabolism
MH  - Animals
MH  - Autophagy/genetics/*physiology
MH  - Autophagy-Related Protein-1 Homolog/genetics/*metabolism
MH  - Autophagy-Related Proteins/genetics/*metabolism
MH  - Humans
MH  - Protein-Tyrosine Kinases/genetics/metabolism
MH  - Vesicular Transport Proteins/genetics/metabolism
PMC - PMC5869855
OTO - NOTNLM
OT  - ULK1
OT  - autophagy
OT  - kinase
COIS- The authors declare that there are no competing interests associated with the 
      manuscript.
EDAT- 2017/12/14 06:00
MHDA- 2018/01/23 06:00
PMCR- 2017/12/12
CRDT- 2017/12/14 06:00
PHST- 2017/09/27 00:00 [received]
PHST- 2017/11/03 00:00 [revised]
PHST- 2017/11/06 00:00 [accepted]
PHST- 2017/12/14 06:00 [entrez]
PHST- 2017/12/14 06:00 [pubmed]
PHST- 2018/01/23 06:00 [medline]
PHST- 2017/12/12 00:00 [pmc-release]
AID - EBC20170021 [pii]
AID - 10.1042/EBC20170021 [doi]
PST - epublish
SO  - Essays Biochem. 2017 Dec 12;61(6):585-596. doi: 10.1042/EBC20170021. Print 2017 
      Dec 12.