Chemical Genetic Screen for AMPKα2 Substrates Uncovers a Network of Proteins Involved in Mitosis

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Chemical Genetic Screen for AMPKα2 Substrates Uncovers a Network of Proteins Involved in Mitosis. / Banko, Max R.; Allen, Jasmina J.; Schaffer, Bethany E.; Wilker, Erik W.; Tsou, Peiling P.; White, Jamie L.; Villén, Judit; Wang, Beatrice; Kim, Sara R.; Sakamoto, Kei; Gygi, Steven P.; Cantley, Lewis C.; Yaffe, Michael B.; Shokat, Kevan M.; Brunet, Anne.

In: Molecular Cell, Vol. 44, No. 6, 23.12.2011, p. 878-892.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Banko, MR, Allen, JJ, Schaffer, BE, Wilker, EW, Tsou, PP, White, JL, Villén, J, Wang, B, Kim, SR, Sakamoto, K, Gygi, SP, Cantley, LC, Yaffe, MB, Shokat, KM & Brunet, A 2011, 'Chemical Genetic Screen for AMPKα2 Substrates Uncovers a Network of Proteins Involved in Mitosis', Molecular Cell, vol. 44, no. 6, pp. 878-892. https://doi.org/10.1016/j.molcel.2011.11.005

APA

Banko, M. R., Allen, J. J., Schaffer, B. E., Wilker, E. W., Tsou, P. P., White, J. L., Villén, J., Wang, B., Kim, S. R., Sakamoto, K., Gygi, S. P., Cantley, L. C., Yaffe, M. B., Shokat, K. M., & Brunet, A. (2011). Chemical Genetic Screen for AMPKα2 Substrates Uncovers a Network of Proteins Involved in Mitosis. Molecular Cell, 44(6), 878-892. https://doi.org/10.1016/j.molcel.2011.11.005

Vancouver

Banko MR, Allen JJ, Schaffer BE, Wilker EW, Tsou PP, White JL et al. Chemical Genetic Screen for AMPKα2 Substrates Uncovers a Network of Proteins Involved in Mitosis. Molecular Cell. 2011 Dec 23;44(6):878-892. https://doi.org/10.1016/j.molcel.2011.11.005

Author

Banko, Max R. ; Allen, Jasmina J. ; Schaffer, Bethany E. ; Wilker, Erik W. ; Tsou, Peiling P. ; White, Jamie L. ; Villén, Judit ; Wang, Beatrice ; Kim, Sara R. ; Sakamoto, Kei ; Gygi, Steven P. ; Cantley, Lewis C. ; Yaffe, Michael B. ; Shokat, Kevan M. ; Brunet, Anne. / Chemical Genetic Screen for AMPKα2 Substrates Uncovers a Network of Proteins Involved in Mitosis. In: Molecular Cell. 2011 ; Vol. 44, No. 6. pp. 878-892.

Bibtex

@article{8799f703717b4de8871e805f49c2067a,
title = "Chemical Genetic Screen for AMPKα2 Substrates Uncovers a Network of Proteins Involved in Mitosis",
abstract = "The energy-sensing AMP-activated protein kinase (AMPK) is activated by low nutrient levels. Functions of AMPK, other than its role in cellular metabolism, are just beginning to emerge. Here we use a chemical genetics screen to identify direct substrates of AMPK in human cells. We find that AMPK phosphorylates 28 previously unidentified substrates, several of which are involved in mitosis and cytokinesis. We identify the residues phosphorylated by AMPK in vivo in several substrates, including protein phosphatase 1 regulatory subunit 12C (PPP1R12C) and p21-activated protein kinase (PAK2). AMPK-induced phosphorylation is necessary for PPP1R12C interaction with 14-3-3 and phosphorylation of myosin regulatory light chain. Both AMPK activity and PPP1R12C phosphorylation are increased in mitotic cells and are important for mitosis completion. These findings suggest that AMPK coordinates nutrient status with mitosis completion, which may be critical for the organism's response to low nutrients during development, or in adult stem and cancer cells.",
author = "Banko, {Max R.} and Allen, {Jasmina J.} and Schaffer, {Bethany E.} and Wilker, {Erik W.} and Tsou, {Peiling P.} and White, {Jamie L.} and Judit Vill{\'e}n and Beatrice Wang and Kim, {Sara R.} and Kei Sakamoto and Gygi, {Steven P.} and Cantley, {Lewis C.} and Yaffe, {Michael B.} and Shokat, {Kevan M.} and Anne Brunet",
year = "2011",
month = dec,
day = "23",
doi = "10.1016/j.molcel.2011.11.005",
language = "English",
volume = "44",
pages = "878--892",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "6",

}

RIS

TY - JOUR

T1 - Chemical Genetic Screen for AMPKα2 Substrates Uncovers a Network of Proteins Involved in Mitosis

AU - Banko, Max R.

AU - Allen, Jasmina J.

AU - Schaffer, Bethany E.

AU - Wilker, Erik W.

AU - Tsou, Peiling P.

AU - White, Jamie L.

AU - Villén, Judit

AU - Wang, Beatrice

AU - Kim, Sara R.

AU - Sakamoto, Kei

AU - Gygi, Steven P.

AU - Cantley, Lewis C.

AU - Yaffe, Michael B.

AU - Shokat, Kevan M.

AU - Brunet, Anne

PY - 2011/12/23

Y1 - 2011/12/23

N2 - The energy-sensing AMP-activated protein kinase (AMPK) is activated by low nutrient levels. Functions of AMPK, other than its role in cellular metabolism, are just beginning to emerge. Here we use a chemical genetics screen to identify direct substrates of AMPK in human cells. We find that AMPK phosphorylates 28 previously unidentified substrates, several of which are involved in mitosis and cytokinesis. We identify the residues phosphorylated by AMPK in vivo in several substrates, including protein phosphatase 1 regulatory subunit 12C (PPP1R12C) and p21-activated protein kinase (PAK2). AMPK-induced phosphorylation is necessary for PPP1R12C interaction with 14-3-3 and phosphorylation of myosin regulatory light chain. Both AMPK activity and PPP1R12C phosphorylation are increased in mitotic cells and are important for mitosis completion. These findings suggest that AMPK coordinates nutrient status with mitosis completion, which may be critical for the organism's response to low nutrients during development, or in adult stem and cancer cells.

AB - The energy-sensing AMP-activated protein kinase (AMPK) is activated by low nutrient levels. Functions of AMPK, other than its role in cellular metabolism, are just beginning to emerge. Here we use a chemical genetics screen to identify direct substrates of AMPK in human cells. We find that AMPK phosphorylates 28 previously unidentified substrates, several of which are involved in mitosis and cytokinesis. We identify the residues phosphorylated by AMPK in vivo in several substrates, including protein phosphatase 1 regulatory subunit 12C (PPP1R12C) and p21-activated protein kinase (PAK2). AMPK-induced phosphorylation is necessary for PPP1R12C interaction with 14-3-3 and phosphorylation of myosin regulatory light chain. Both AMPK activity and PPP1R12C phosphorylation are increased in mitotic cells and are important for mitosis completion. These findings suggest that AMPK coordinates nutrient status with mitosis completion, which may be critical for the organism's response to low nutrients during development, or in adult stem and cancer cells.

UR - http://www.scopus.com/inward/record.url?scp=84355161919&partnerID=8YFLogxK

U2 - 10.1016/j.molcel.2011.11.005

DO - 10.1016/j.molcel.2011.11.005

M3 - Journal article

C2 - 22137581

AN - SCOPUS:84355161919

VL - 44

SP - 878

EP - 892

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 6

ER -

ID: 239567781