4.7 Review

Protein Localization at Mitochondria-ER Contact Sites in Basal and Stress Conditions

Journal

Publisher

FRONTIERS MEDIA SA
DOI: 10.3389/fcell.2017.00107

Keywords

mitochondria-ER contact sites; protein targeting; post-translational modifications; lipid rafts; ER stress

Funding

  1. CARIPARO Starting Grant 2016 AIFbiol
  2. DiBio Departmental Research Project PRID Seed 2017
  3. MINECO (Spanish Ministry of Economy and Competitiveness) [SAF2014-51876-R]
  4. Worldwide Cancer Research Foundation [15-0404]
  5. IPP-CNIC postdoctoral fellow award
  6. Spanish Ministry of Economy and Competitiveness (MINECO)
  7. Pro-CNIC Foundation
  8. Severo Ochoa Center of Excellence [SEV-2015-0505]
  9. Worldwide Cancer Research [15-0404] Funding Source: researchfish

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Mitochondria-endoplasmic reticulum (ER) contacts (MERCs) are sites at which the outer mitochondria membrane and the Endoplasmic Reticulum surface run in parallel at a constant distance. The juxtaposition between these organelles determines several intracellular processes such as to name a few, Ca2+ and lipid homeostasis or autophagy. These specific tasks can be exploited thanks to the enrichment (or re-localization) of dedicated proteins at these interfaces. Recent proteomic studies highlight the tissue specific composition of MERCs, but the overall mechanisms that control MERCs plasticity remains unclear. Understanding how proteins are targeted at these sites seems pivotal to clarify such contextual function of MERCs. This review aims to summarize the current knowledge on protein localization at MERCs and the possible contribution of the mislocalization of MERCs components to human disorders.

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