PMID- 32516305
OWN - NLM
STAT- MEDLINE
DCOM- 20200723
LR  - 20231111
IS  - 1545-7885 (Electronic)
IS  - 1544-9173 (Print)
IS  - 1544-9173 (Linking)
VI  - 18
IP  - 6
DP  - 2020 Jun
TI  - Mitotic phosphorylation of the ULK complex regulates cell cycle progression.
PG  - e3000718
LID - 10.1371/journal.pbio.3000718 [doi]
LID - e3000718
AB  - Autophagy is an intracellular degradation pathway targeting organelles and 
      macromolecules, thereby regulating various cellular functions. Phosphorylation is 
      a key posttranscriptional protein modification implicated in the regulation of 
      biological function including autophagy. Under asynchronous conditions, autophagy 
      activity is predominantly suppressed by mechanistic target of rapamycin (mTOR) 
      kinase, but whether autophagy-related genes (ATG) proteins are phosphorylated 
      differentially throughout the sequential phases of the cell cycle remains 
      unclear. In this issue, Li and colleagues report that cyclin-dependent kinase 1 
      (CDK1) phosphorylates the ULK complex during mitosis. This phosphorylation 
      induces autophagy and, surprisingly, is shown to drive cell cycle progression. 
      This work reveals a yet-unappreciated role for autophagy in cell cycle 
      progression and enhances our understanding of the specific phase-dependent 
      autophagy regulation during cellular growth and proliferation.
FAU - Yamasaki, Akinori
AU  - Yamasaki A
AUID- ORCID: 0000-0002-5820-5549
AD  - Cell Biology Center, Institute of Innovative Research, Tokyo Institute of 
      Technology, Yokohama, Japan.
FAU - Jin, Yui
AU  - Jin Y
AUID- ORCID: 0000-0001-6551-5775
AD  - Cell Biology Center, Institute of Innovative Research, Tokyo Institute of 
      Technology, Yokohama, Japan.
AD  - Tokyo Tech World Research Hub Initiative (WRHI), Institute of Innovative 
      Research, Tokyo Institute of Technology, Yokohama, Japan.
FAU - Ohsumi, Yoshinori
AU  - Ohsumi Y
AD  - Cell Biology Center, Institute of Innovative Research, Tokyo Institute of 
      Technology, Yokohama, Japan.
LA  - eng
PT  - Comment
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20200609
PL  - United States
TA  - PLoS Biol
JT  - PLoS biology
JID - 101183755
RN  - EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1)
RN  - EC 2.7.11.1 (TOR Serine-Threonine Kinases)
RN  - EC 2.7.11.22 (CDC2 Protein Kinase)
SB  - IM
CON - Mol Cell. 2020 Jan 16;77(2):228-240.e7. PMID: 31733992
CON - PLoS Biol. 2020 Jun 9;18(6):e3000288. PMID: 32516310
MH  - *Autophagy
MH  - *CDC2 Protein Kinase
MH  - Mechanistic Target of Rapamycin Complex 1
MH  - Mitosis
MH  - Phosphorylation
MH  - TOR Serine-Threonine Kinases
PMC - PMC7282621
COIS- The authors have declared that no competing interests exist.
EDAT- 2020/06/10 06:00
MHDA- 2020/07/24 06:00
PMCR- 2020/06/09
CRDT- 2020/06/10 06:00
PHST- 2020/06/10 06:00 [entrez]
PHST- 2020/06/10 06:00 [pubmed]
PHST- 2020/07/24 06:00 [medline]
PHST- 2020/06/09 00:00 [pmc-release]
AID - PBIOLOGY-D-20-00745 [pii]
AID - 10.1371/journal.pbio.3000718 [doi]
PST - epublish
SO  - PLoS Biol. 2020 Jun 9;18(6):e3000718. doi: 10.1371/journal.pbio.3000718. 
      eCollection 2020 Jun.