Topical Collection "Feature Papers in Organelle Function"

A topical collection in Cells (ISSN 2073-4409). This collection belongs to the section "Organelle Function".

Editor

Prof. Paolo Bernardi
E-Mail
Collection Editor
Department of Biomedical Sciences, University of Padova, Via Ugo Bassi 58/B, I-35131 Padova, Italy
Interests: mitochondria; calcium; channels; permeability transition; ATP synthase; cell death
Special Issues and Collections in MDPI journals

Topical Collection Information

Dear Colleagues,

This Topical Collection entitled “Feature Papers in Organelle Function” aims to collect high-quality research articles, communications, and review articles in the key field of organelle function. Since the aim of this Topical Collection is to illustrate frontier research in organelle function through selected works, we encourage Editorial Board Members of Cells to contribute papers reflecting the latest progress in their research field, or relevant experts and colleagues to do so. Please kindly note that all invited papers will be published online with discounts or free of charge once accepted.

We welcome the submission of manuscripts that deal with specific aspects of organelle physiology or that help deciphering how subcellular structures are maintained in the face of membrane flow and how individual organelles send and receive specific information to maintain intracellular homeostasis.

Topics of interest include, but are not limited to:

  • cell membrane
  • cell wall
  • centrioles
  • chloroplasts
  • cytoplasm
  • cytoskeleton
  • endoplasmic reticulum
  • Golgi apparatus
  • intracellular vesicles
  • lysosomes
  • microfilaments
  • microtubules
  • mitochondria
  • nuclei
  • nucleoli
  • peroxisomes
  • ribosomes
  • vacuoles
  • Lipid

Prof. Paolo Bernardi
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the collection website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Cells is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2000 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Published Papers (2 papers)

2020

Open AccessFeature PaperArticle
A Novel FRET Approach Quantifies the Interaction Strength of Peroxisomal Targeting Signals and Their Receptor in Living Cells
Cells 2020, 9(11), 2381; https://doi.org/10.3390/cells9112381 - 30 Oct 2020
Viewed by 773
Abstract
Measuring Förster–resonance–energy–transfer (FRET) efficiency allows the investigation of protein–protein interactions (PPI), but extracting quantitative measures of affinity necessitates highly advanced technical equipment or isolated proteins. We demonstrate the validity of a recently suggested novel approach to quantitatively analyze FRET-based experiments in living mammalian [...] Read more.
Measuring Förster–resonance–energy–transfer (FRET) efficiency allows the investigation of protein–protein interactions (PPI), but extracting quantitative measures of affinity necessitates highly advanced technical equipment or isolated proteins. We demonstrate the validity of a recently suggested novel approach to quantitatively analyze FRET-based experiments in living mammalian cells using standard equipment using the interaction between different type-1 peroxisomal targeting signals (PTS1) and their soluble receptor peroxin 5 (PEX5) as a model system. Large data sets were obtained by flow cytometry coupled FRET measurements of cells expressing PTS1-tagged EGFP together with mCherry fused to the PTS1-binding domain of PEX5, and were subjected to a fitting algorithm extracting a quantitative measure of the interaction strength. This measure correlates with results obtained by in vitro techniques and a two-hybrid assay, but is unaffected by the distance between the fluorophores. Moreover, we introduce a live cell competition assay based on this approach, capable of depicting dose- and affinity-dependent modulation of the PPI. Using this system, we demonstrate the relevance of a sequence element next to the core tripeptide in PTS1 motifs for the interaction strength between PTS1 and PEX5, which is supported by a structure-based computational prediction of the binding energy indicating a direct involvement of this sequence in the interaction. Full article
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Graphical abstract

Open AccessArticle
Transmembrane BAX Inhibitor-1 Motif Containing Protein 5 (TMBIM5) Sustains Mitochondrial Structure, Shape, and Function by Impacting the Mitochondrial Protein Synthesis Machinery
Cells 2020, 9(10), 2147; https://doi.org/10.3390/cells9102147 - 23 Sep 2020
Cited by 1 | Viewed by 1001
Abstract
The Transmembrane Bax Inhibitor-1 motif (TMBIM)-containing protein family is evolutionarily conserved and has been implicated in cell death susceptibility. The only member with a mitochondrial localization is TMBIM5 (also known as GHITM or MICS1), which affects cristae organization and associates with the Parkinson’s [...] Read more.
The Transmembrane Bax Inhibitor-1 motif (TMBIM)-containing protein family is evolutionarily conserved and has been implicated in cell death susceptibility. The only member with a mitochondrial localization is TMBIM5 (also known as GHITM or MICS1), which affects cristae organization and associates with the Parkinson’s disease-associated protein CHCHD2 in the inner mitochondrial membrane. We here used CRISPR-Cas9-mediated knockout HAP1 cells to shed further light on the function of TMBIM5 in physiology and cell death susceptibility. We found that compared to wild type, TMBIM5-knockout cells were smaller and had a slower proliferation rate. In these cells, mitochondria were more fragmented with a vacuolar cristae structure. In addition, the mitochondrial membrane potential was reduced and respiration was attenuated, leading to a reduced mitochondrial ATP generation. TMBIM5 did not associate with Mic10 and Mic60, which are proteins of the mitochondrial contact site and cristae organizing system (MICOS), nor did TMBIM5 knockout affect their expression levels. TMBIM5-knockout cells were more sensitive to apoptosis elicited by staurosporine and BH3 mimetic inhibitors of Bcl-2 and Bcl-XL. An unbiased proteomic comparison identified a dramatic downregulation of proteins involved in the mitochondrial protein synthesis machinery in TMBIM5-knockout cells. We conclude that TMBIM5 is important to maintain the mitochondrial structure and function possibly through the control of mitochondrial biogenesis. Full article
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Figure 1

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