Feature Papers in Biological Membrane Composition and Structures

A topical collection in Membranes (ISSN 2077-0375).

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Editor


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Collection Editor
1. Division of Biological Science, Graduate School of Science and Technology, Nara Institute of Science and Technology, Nara 630-0192, Japan
2. Data Science Center, Nara Institute of Science and Technology, Nara 630-0192, Japan
3. Center for Digital Green-Innovation, Nara Institute of Science and Technology, Nara 630-0192, Japan
Interests: mechanisms of cell shaping and cell fate determination
Special Issues, Collections and Topics in MDPI journals

Topical Collection Information

Dear Colleagues,

Biological membranes, which include cellular membranes and membrane particles derived from cells, are an essential component of life. Biological membranes consist of various lipids and embedded or associated proteins with or without modifications by sugar and different other materials. The structure of the biological membrane is the result of the assembly of such a variety of materials and exhibits the structure for their functions. This feature paper collection will include but are not limited to:

  • The reconstitution studies of the biological membrane components,
  • The subcellular organelle studies,
  • The extracellular vesicles studies,
  • The membrane-embedded/associated protein studies
  • Membrane shaping of cells
  • Membrane shaping of subcellular organelles
  • Membrane shaping of artificial liposomes
  • Transport across membranes
  • Cell function related to membrane morphogenesis
  • Transport by membrane vesicles
  • Membrane interaction with proteins, sugars, and other biological materials
  • Biological membrane synthesis
  • Application of biological membranes and mimicry in industry and research
  • Visualization of membranes.

Prof. Dr. Shiro Suetsugu
Collection 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 submissions that pass pre-check are 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. Membranes 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 2700 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)

2024

Jump to: 2023

16 pages, 4363 KiB  
Article
Membrane-Associated Ubiquitin Ligase RING Finger Protein 152 Orchestrates Melanogenesis via Tyrosinase Ubiquitination
by Ryota Ueda, Rina Hashimoto, Yuki Fujii, José C. J. M. D. S. Menezes, Hirotaka Takahashi, Hiroyuki Takeda, Tatsuya Sawasaki, Tomonori Motokawa, Kenzo Tokunaga and Hideaki Fujita
Membranes 2024, 14(2), 43; https://doi.org/10.3390/membranes14020043 - 1 Feb 2024
Viewed by 2171
Abstract
Lysosomal degradation of tyrosinase, a pivotal enzyme in melanin synthesis, negatively impacts melanogenesis in melanocytes. Nevertheless, the precise molecular mechanisms by which lysosomes target tyrosinase have remained elusive. Here, we identify RING (Really Interesting New Gene) finger protein 152 (RNF152) as a membrane-associated [...] Read more.
Lysosomal degradation of tyrosinase, a pivotal enzyme in melanin synthesis, negatively impacts melanogenesis in melanocytes. Nevertheless, the precise molecular mechanisms by which lysosomes target tyrosinase have remained elusive. Here, we identify RING (Really Interesting New Gene) finger protein 152 (RNF152) as a membrane-associated ubiquitin ligase specifically targeting tyrosinase for the first time, utilizing AlphaScreen technology. We observed that modulating RNF152 levels in B16 cells, either via overexpression or siRNA knockdown, resulted in decreased or increased levels of both tyrosinase and melanin, respectively. Notably, RNF152 and tyrosinase co-localized at the trans-Golgi network (TGN). However, upon treatment with lysosomal inhibitors, both proteins appeared in the lysosomes, indicating that tyrosinase undergoes RNF152-mediated lysosomal degradation. Through ubiquitination assays, we found the indispensable roles of both the RING and transmembrane (TM) domains of RNF152 in facilitating tyrosinase ubiquitination. In summary, our findings underscore RNF152 as a tyrosinase-specific ubiquitin ligase essential for regulating melanogenesis in melanocytes. Full article
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Graphical abstract

2023

Jump to: 2024

11 pages, 2816 KiB  
Article
Assembly of Cell-Free Synthesized Ion Channel Molecules in Artificial Lipid Bilayer Observed by Atomic Force Microscopy
by Melvin Wei Shern Goh, Yuzuru Tozawa and Ryugo Tero
Membranes 2023, 13(11), 854; https://doi.org/10.3390/membranes13110854 - 25 Oct 2023
Viewed by 1574
Abstract
Artificial lipid bilayer systems, such as vesicles, black membranes, and supported lipid bilayers (SLBs), are valuable platforms for studying ion channels at the molecular level. The reconstitution of the ion channels in an active form is a crucial process in studies using artificial [...] Read more.
Artificial lipid bilayer systems, such as vesicles, black membranes, and supported lipid bilayers (SLBs), are valuable platforms for studying ion channels at the molecular level. The reconstitution of the ion channels in an active form is a crucial process in studies using artificial lipid bilayer systems. In this study, we investigated the assembly of the human ether-a-go-go-related gene (hERG) channel prepared in a cell-free synthesis system. AFM topographies revealed the presence of protrusions with a uniform size in the entire SLB that was prepared with the proteoliposomes (PLs) incorporating the cell-free-synthesized hERG channel. We attributed the protrusions to hERG channel monomers, taking into consideration the AFM tip size, and identified assembled structures of the monomer that exhibited dimeric, trimeric, and tetrameric-like arrangements. We observed molecular images of the functional hERG channel reconstituted in a lipid bilayer membrane using AFM and quantitatively evaluated the association state of the cell-free synthesized hERG channel. Full article
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Figure 1

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