Literature DB >> 27456366

Reconstitutions of mitochondrial inner membrane remodeling.

Mariam Barbot1, Michael Meinecke2.   

Abstract

Biological membranes exhibit function-related shapes, leading to a plethora of complex and beautiful cell and cell organellar morphologies. Most if not all of these structures have evolved for a particular physiological reason. The shapes of these structures are formed by physical forces that operate on membranes. To create particular shaped cells and cell organelles, membranes must undergo deformations which are determined by the structure and elasticity of the membrane and this process is most probable driven by proteins, lipids and/or interplay of both Zimmerberg and Kozlov (2006). Therefore, an important question of current cell biology in conjunction with physics and mathematics is to elucidate the functional cause for these different membrane morphologies as well as how they are formed. One of the most peculiar membrane shapes is observed in mitochondria. These organelles are surrounded by two membranes and especially the convoluted inner membrane displays a complex ultra-structure. A molecular understanding of how this membrane is shaped is missing to a large extent. Unlike membrane remodeling in classical curvature-dependent processes like clathrin-mediated endocytosis, mitochondria are most likely shaped by integral membrane proteins. Following, we will review the current knowledge of inner mitochondrial membrane architecture and discuss recent findings and advances in understanding the factors that shape this membrane. We will address pending questions especially with regard to the experimentally challenging nature of investigating membrane bending by hydrophobic integral membrane proteins.
Copyright © 2016 Elsevier Inc. All rights reserved.

Entities:  

Keywords:  MICOS; Membrane curvature; Membrane dynamics; Mic10; Mitochondria

Mesh:

Substances:

Year:  2016        PMID: 27456366     DOI: 10.1016/j.jsb.2016.07.014

Source DB:  PubMed          Journal:  J Struct Biol        ISSN: 1047-8477            Impact factor:   2.867


  6 in total

1.  The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology.

Authors:  Daryna Tarasenko; Mariam Barbot; Daniel C Jans; Benjamin Kroppen; Boguslawa Sadowski; Gudrun Heim; Wiebke Möbius; Stefan Jakobs; Michael Meinecke
Journal:  J Cell Biol       Date:  2017-03-02       Impact factor: 10.539

Review 2.  Protein-dependent membrane remodeling in mitochondrial morphology and clathrin-mediated endocytosis.

Authors:  Daryna Tarasenko; Michael Meinecke
Journal:  Eur Biophys J       Date:  2021-02-02       Impact factor: 1.733

3.  Cation selectivity of the presequence translocase channel Tim23 is crucial for efficient protein import.

Authors:  Niels Denkert; Alexander Benjamin Schendzielorz; Mariam Barbot; Lennart Versemann; Frank Richter; Peter Rehling; Michael Meinecke
Journal:  Elife       Date:  2017-08-31       Impact factor: 8.140

4.  Coordinated organization of mitochondrial lamellar cristae and gain of COX function during mitochondrial maturation in Drosophila.

Authors:  Yi-Fan Jiang; Hsiang-Ling Lin; Li-Jie Wang; Tian Hsu; Chi-Yu Fu
Journal:  Mol Biol Cell       Date:  2019-11-20       Impact factor: 4.138

5.  Cooperativity of membrane-protein and protein-protein interactions control membrane remodeling by epsin 1 and affects clathrin-mediated endocytosis.

Authors:  Benjamin Kroppen; Nelli Teske; King F Yambire; Niels Denkert; Indrani Mukherjee; Daryna Tarasenko; Garima Jaipuria; Markus Zweckstetter; Ira Milosevic; Claudia Steinem; Michael Meinecke
Journal:  Cell Mol Life Sci       Date:  2020-09-30       Impact factor: 9.261

Review 6.  Emerging Roles of the MICOS Complex in Cristae Dynamics and Biogenesis.

Authors:  Ruchika Anand; Andreas S Reichert; Arun Kumar Kondadi
Journal:  Biology (Basel)       Date:  2021-06-29
  6 in total

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