AMPK-dependent activation of the Cyclin Y/CDK16 complex controls autophagy
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AMPK-dependent activation of the Cyclin Y/CDK16 complex controls autophagy. / Dohmen, Marc; Krieg, Sarah; Agalaridis, Georgios; Zhu, Xiaoqing; Shehata, Saifeldin N; Pfeiffenberger, Elisabeth; Amelang, Jan; Bütepage, Mareike; Buerova, Elena; Pfaff, Carolina M; Chanda, Dipanjan; Geley, Stephan; Preisinger, Christian; Sakamoto, Kei; Lüscher, Bernhard; Neumann, Dietbert; Vervoorts, Jörg.
I: Nature Communications, Bind 11, Nr. 1, 1032, 2020.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › fagfællebedømt
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TY - JOUR
T1 - AMPK-dependent activation of the Cyclin Y/CDK16 complex controls autophagy
AU - Dohmen, Marc
AU - Krieg, Sarah
AU - Agalaridis, Georgios
AU - Zhu, Xiaoqing
AU - Shehata, Saifeldin N
AU - Pfeiffenberger, Elisabeth
AU - Amelang, Jan
AU - Bütepage, Mareike
AU - Buerova, Elena
AU - Pfaff, Carolina M
AU - Chanda, Dipanjan
AU - Geley, Stephan
AU - Preisinger, Christian
AU - Sakamoto, Kei
AU - Lüscher, Bernhard
AU - Neumann, Dietbert
AU - Vervoorts, Jörg
PY - 2020
Y1 - 2020
N2 - The AMP-activated protein kinase (AMPK) is a master sensor of the cellular energy status that is crucial for the adaptive response to limited energy availability. AMPK is implicated in the regulation of many cellular processes, including autophagy. However, the precise mechanisms by which AMPK controls these processes and the identities of relevant substrates are not fully understood. Using protein microarrays, we identify Cyclin Y as an AMPK substrate that is phosphorylated at Serine 326 (S326) both in vitro and in cells. Phosphorylation of Cyclin Y at S326 promotes its interaction with the Cyclin-dependent kinase 16 (CDK16), thereby stimulating its catalytic activity. When expressed in cells, Cyclin Y/CDK16 is sufficient to promote autophagy. Moreover, Cyclin Y/CDK16 is necessary for efficient AMPK-dependent activation of autophagy. This functional interaction is mediated by AMPK phosphorylating S326 of Cyclin Y. Collectively, we define Cyclin Y/CDK16 as downstream effector of AMPK for inducing autophagy.
AB - The AMP-activated protein kinase (AMPK) is a master sensor of the cellular energy status that is crucial for the adaptive response to limited energy availability. AMPK is implicated in the regulation of many cellular processes, including autophagy. However, the precise mechanisms by which AMPK controls these processes and the identities of relevant substrates are not fully understood. Using protein microarrays, we identify Cyclin Y as an AMPK substrate that is phosphorylated at Serine 326 (S326) both in vitro and in cells. Phosphorylation of Cyclin Y at S326 promotes its interaction with the Cyclin-dependent kinase 16 (CDK16), thereby stimulating its catalytic activity. When expressed in cells, Cyclin Y/CDK16 is sufficient to promote autophagy. Moreover, Cyclin Y/CDK16 is necessary for efficient AMPK-dependent activation of autophagy. This functional interaction is mediated by AMPK phosphorylating S326 of Cyclin Y. Collectively, we define Cyclin Y/CDK16 as downstream effector of AMPK for inducing autophagy.
U2 - 10.1038/s41467-020-14812-0
DO - 10.1038/s41467-020-14812-0
M3 - Journal article
C2 - 32098961
VL - 11
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
IS - 1
M1 - 1032
ER -
ID: 239920775