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The SEACIT complex is involved in the maintenance of vacuole–mitochondria contact sites and controls mitophagy

  • Yinxing Ma
  • Alexis Moors
  • Nadine Camougrand
  • Svetlana DokudovskayaEmail author
Original Article

Abstract

The major signaling pathway that regulates cell growth and metabolism is under the control of the target of rapamycin complex 1 (TORC1). In Saccharomyces cerevisiae the SEA complex is one of the TORC1 upstream regulators involved in amino acid sensing and autophagy. Here, we performed analysis of the expression, interactions and localization of SEA complex proteins under different conditions, varying parameters such as sugar source, nitrogen availability and growth phase. Our results show that the SEA complex promotes mitochondria degradation either by mitophagy or by general autophagy. In addition, the SEACIT subcomplex is involved in the maintenance of the vacuole–mitochondria contact sites. Thus, the SEA complex appears to be an important link between the TORC1 pathway and regulation of mitochondria quality control.

Keywords

Membrane contact sites Vacuole Mitochondria SEA complex TORC1 Autophagy Mitophagy 

Abbreviations

ROS

Reactive oxygen species

SEACAT

SEA subcomplex activating TORC1

SEACIT

SEA subcomplex inhibiting TORC1

TORC1

Target of rapamycin complex 1

vCLAMPs

Vacuole–mitochondria contact sites

Notes

Acknowledgements

We are grateful to Jaclyn Tetenbaum-Novatt and Renaud Legouis for critical reading of manuscript. We thank Sebastien Leon, Christian Ungermann, Benedikt Westermann and Claudio de Virgilio for sharing plasmids and antibodies.

Funding

SD acknowledge financial support from La Ligue contre le Cancer (Comité de Paris/Ile-de-France and Comité d’Oise), PICS USA (CNRS); YM is grateful to the support from Chinese Scholarship Council (CSC). We thank Proteomic Core Facility (support from grants TA2013 and TA2016), Imaging and Cytometry Facility (PFIC, UMS CNRS 3655—INSERM US23, support from grant TA2017).

Compliance with ethical standards

Conflict of interest

The authors declare no competing interests

Supplementary material

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Copyright information

© Springer Nature Switzerland AG 2019

Authors and Affiliations

  1. 1.CNRS, UMR 8126, Université Paris-Sud 11, Institut Gustave RoussyVillejuifFrance
  2. 2.CNRS, IBGC, UMR 5095BordeauxFrance
  3. 3.Université de Bordeaux, IBGCBordeauxFrance

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