Role of MINOS in mitochondrial membrane architecture and biogenesis

Martin van der Laan1, Maria Bohnert, Nils Wiedemann

  • 1Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung, Universität Freiburg, 79104 Freiburg, Germany.

Insights

Mitochondrial inner-membrane organizing system (MINOS) is key to mitochondrial architecture. We propose MINOS is part of a larger ER-mitochondria organizing network (ERMIONE) controlling membrane structure and biogenesis.

Area of Science:

  • Cell Biology
  • Mitochondrial Biology
  • Membrane Biology

Background:

  • Mitochondria have a complex, two-membrane structure.
  • The inner mitochondrial membrane comprises boundary and crista domains connected by crista junctions.
  • The mitochondrial inner-membrane organizing system (MINOS) complex is known to be crucial for inner membrane architecture.

Purpose of the Study:

  • To propose a new network model for mitochondrial membrane organization.
  • To investigate the role of MINOS in relation to the endoplasmic reticulum (ER).

Main Methods:

  • Literature review and synthesis of recent findings.
  • Conceptual modeling of protein complex interactions.

Main Results:

  • MINOS interacts with outer membrane protein translocases.
  • These translocases are linked to ER-mitochondria contact sites.
  • A model is proposed where MINOS is central to an ER-mitochondria organizing network (ERMIONE).

Conclusions:

  • ERMIONE integrates MINOS function with ER-mitochondria communication.
  • This network likely controls mitochondrial membrane architecture and biogenesis.
  • Further research is needed to experimentally validate the ERMIONE model.

Related Concept Videos

The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Mitochondrial Membranes01:45

Mitochondrial Membranes

A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
Mitochondrial Membranes01:45

Mitochondrial Membranes

A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...