Cell-autonomous control of intracellular temperature by unsaturation of phospholipid acyl chains

Akira Murakami; Kohjiro Nagao; Reiko Sakaguchi; Keisuke Kida; Yuji Hara; Yasuo Mori; Kohki Okabe; Yoshie Harada; Masato Umeda

doi:10.1016/j.celrep.2022.110487

Cell-autonomous control of intracellular temperature by unsaturation of phospholipid acyl chains

Cell Rep. 2022 Mar 15;38(11):110487. doi: 10.1016/j.celrep.2022.110487.

Authors

Akira Murakami¹, Kohjiro Nagao², Reiko Sakaguchi³, Keisuke Kida³, Yuji Hara³, Yasuo Mori³, Kohki Okabe⁴, Yoshie Harada⁵, Masato Umeda⁶

Affiliations

¹ Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Kyoto 615-8510, Japan; Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japan.
² Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Kyoto 615-8510, Japan. Electronic address: nagao-k@mb.kyoto-phu.ac.jp.
³ Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Kyoto 615-8510, Japan.
⁴ Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japan.
⁵ Institute for Protein Research, Osaka University, Osaka 565-0871, Japan.
⁶ Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Kyoto 615-8510, Japan. Electronic address: umeda@sbchem.kyoto-u.ac.jp.

PMID: 35294880
DOI: 10.1016/j.celrep.2022.110487

Abstract

Intracellular temperature affects a wide range of cellular functions in living organisms. However, it remains unclear whether temperature in individual animal cells is controlled autonomously as a response to fluctuations in environmental temperature. Using two distinct intracellular thermometers, we find that the intracellular temperature of steady-state Drosophila S2 cells is maintained in a manner dependent on Δ9-fatty acid desaturase DESAT1, which introduces a double bond at the Δ9 position of the acyl moiety of acyl-CoA. The DESAT1-mediated increase of intracellular temperature is caused by the enhancement of F₁F_o-ATPase-dependent mitochondrial respiration, which is coupled with thermogenesis. We also reveal that F₁F_o-ATPase-dependent mitochondrial respiration is potentiated by cold exposure through the remodeling of mitochondrial cristae structures via DESAT1-dependent unsaturation of mitochondrial phospholipid acyl chains. Based on these findings, we propose a cell-autonomous mechanism for intracellular temperature control during environmental temperature changes.

Keywords: F(1)F(o)-ATPase; intracellular temperature; mitochondrial cristae; mitochondrial thermogenesis; phospholipid; Δ9-fatty acid desaturase.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Adenosine Triphosphatases
Animals
Drosophila
Fatty Acid Desaturases*
Phospholipids*
Stearoyl-CoA Desaturase
Temperature

Substances

Phospholipids
Fatty Acid Desaturases
Stearoyl-CoA Desaturase
Adenosine Triphosphatases