Nutrient-dependent acetylation controls basic regulatory metabolic switches and cellular reprogramming
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Nutrient-dependent acetylation controls basic regulatory metabolic switches and cellular reprogramming. / Dominy, J. E.; Gerhart-Hines, Z.; Puigserver, P.
In: Cold Spring Harbor Symposia on Quantitative Biology, Vol. 76, 2011, p. 203-209.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Nutrient-dependent acetylation controls basic regulatory metabolic switches and cellular reprogramming
AU - Dominy, J. E.
AU - Gerhart-Hines, Z.
AU - Puigserver, P.
PY - 2011
Y1 - 2011
N2 - Organisms must be able to selectively tailor their ability to use the macronutrients of carbohydrate, protein, and fat based on their availability. In different cell types, how the nutrient fluctuations are sensed and the mechanisms by which the pathways of central metabolism are switched to favor the use of one particular nutrient type over another are topics of intense interest. Protein acetylation is one major evolutionary conserved mechanism by which nutrient fluctuations are sensed within cells and subsequently coupled with metabolic switching. In this review, we present the case of PGC-1α acetylation and how the control of PGC-1α's activity by acetylation sets into motion a wide range of metabolic adaptations that makes this protein an exemplary model for acetylation-mediated mechanisms of nutrient sensing and communication.
AB - Organisms must be able to selectively tailor their ability to use the macronutrients of carbohydrate, protein, and fat based on their availability. In different cell types, how the nutrient fluctuations are sensed and the mechanisms by which the pathways of central metabolism are switched to favor the use of one particular nutrient type over another are topics of intense interest. Protein acetylation is one major evolutionary conserved mechanism by which nutrient fluctuations are sensed within cells and subsequently coupled with metabolic switching. In this review, we present the case of PGC-1α acetylation and how the control of PGC-1α's activity by acetylation sets into motion a wide range of metabolic adaptations that makes this protein an exemplary model for acetylation-mediated mechanisms of nutrient sensing and communication.
UR - http://www.scopus.com/inward/record.url?scp=84867414867&partnerID=8YFLogxK
U2 - 10.1101/sqb.2012.76.010843
DO - 10.1101/sqb.2012.76.010843
M3 - Journal article
C2 - 22371372
AN - SCOPUS:84867414867
VL - 76
SP - 203
EP - 209
JO - Cold Spring Harbor Laboratory. Symposia on Quantitative Biology
JF - Cold Spring Harbor Laboratory. Symposia on Quantitative Biology
SN - 0091-7451
ER -
ID: 347796196