Of yeast, mice and men: MAMs come in two flavors

Maria Sol Herrera-Cruz1, Thomas Simmen2

  • 1Department of Cell Biology, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, T6G2H7, Canada.

Biology Direct
|January 27, 2017
PubMed

Insights

Membrane contact sites (MCS) between the endoplasmic reticulum and mitochondria, known as MAMs, have distinct mechanisms in yeast and mammals. This review explores these differences to resolve conflicting research findings.

Area of Science:

  • Cell Biology
  • Molecular Biology

Background:

  • Membrane contact sites (MCS) are crucial for cellular functions.
  • Endoplasmic reticulum (ER)-mitochondria contact sites, termed mitochondria-associated membranes (MAMs), were first identified in mammals.
  • MAMs have since been discovered in yeast (Saccharomyces cerevisiae), revealing novel tethering complexes like ERMES.

Purpose of the Study:

  • To review and compare the mechanistic differences between yeast and mammalian MAMs.
  • To elucidate the underlying causes of discrepancies in findings between these model systems.
  • To provide insights into the conserved and divergent functions of ER-mitochondria contacts.

Main Methods:

  • Comparative analysis of literature on MAMs in yeast and mammalian systems.
  • Identification and discussion of key MAM proteins and tethering complexes (e.g., PACS-2, mitofusin-2, ERMES, Gem1, Lam6).
  • Examination of functional differences in lipid metabolism, Ca2+ signaling, and other processes.

Main Results:

  • Mammalian and yeast MAMs exhibit significant mechanistic variations.
  • Novel yeast-specific tethers (ERMES) and conserved regulators (Gem1, Lam6) have been identified.
  • Functional roles of MAMs, including lipid metabolism and Ca2+ signaling, differ between species.

Conclusions:

  • Understanding species-specific MAM mechanisms is essential for reconciling research.
  • Divergent MAM structures and functions impact cellular processes differently in yeast and mammals.
  • Further research is needed to fully characterize the conserved and unique aspects of ER-mitochondria communication.