Special Issue "Biological Membrane Morphogenesis"

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A special issue of Membranes (ISSN 2077-0375). This special issue belongs to the section "Biological Membranes (Transport Processes)".

Deadline for manuscript submissions: closed (31 October 2011)

Special Issue Editor

Guest Editor
Prof. Dr. Shiro Suetsugu (Website)

Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5, Takayama, Ikoma, Nara, 630-0192, Japan
Fax: +81 3 5841 7862
Interests: cellular membrane curvatures; cellular membrane structures; protein-lipid interactions; lipid signaling in cells; membrane morphology

Special Issue Information

Dear Colleagues,

The first issue of the journal Membrane is started in 2011. Besides those of chemical and industrial fields, Membranes also covers the biological membranes in medical and basic biology fields.

The membranes of living cells are composed of lipid bilayer, and have specific morphologies that are recognized as sub-cellular structures such as ER, golgi apparatus, coated pits, coated vesicles, filopodia, lamellipodia, and so on. However, reconstituted biological membranes from cells or tissues are unable to adapt to such specific morphology because of the fluidity of the membrane. The morphology of biological membranes is shaped and maintained by membrane binding proteins that bend the membrane or modify lipid composition of the membrane. This special issue will focus on the proteins that can shape the biological membranes.

We are seeking papers for this special issue of Membranes that reflect recent advances in the understanding the mechanism of sub-cellular morphogenesis of cellular membrane. Both review and original research articles are welcome to the special issue.

Prof. Dr. Shiro Suetsugu
Guest Editor

Keywords

  • membrane binding proteins
  • membrane curvature
  • membrane morphology
  • actin cytoskeleton
  • protein-lipid interactions
  • lipid asymmetry of membrane
  • clathrin
  • caveolae
  • filopodia
  • lamellipodia

Published Papers (5 papers)

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Research

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Open AccessArticle Formation of Oligovesicular Vesicles by Micromanipulation
Membranes 2011, 1(4), 265-274; doi:10.3390/membranes1040265
Received: 7 September 2011 / Revised: 20 September 2011 / Accepted: 21 September 2011 / Published: 26 September 2011
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Abstract
Cell-sized lipid bilayer membrane vesicles (giant vesicles, GVs) or semi-vesicles were formed from egg yolk phosphatidylcholine on a platinum electrode under applied electric voltage by electroformation. Micromanipulation of the semi-vesicle by first pressing its membrane with a glass microneedle and then withdrawing [...] Read more.
Cell-sized lipid bilayer membrane vesicles (giant vesicles, GVs) or semi-vesicles were formed from egg yolk phosphatidylcholine on a platinum electrode under applied electric voltage by electroformation. Micromanipulation of the semi-vesicle by first pressing its membrane with a glass microneedle and then withdrawing the needle left a GV in the interior of the vesicle. During the process, an aqueous solution of Ficoll that filled the needle was introduced into the newly formed inner vesicle and remained encapsulated. Approximately 50% of attempted micromanipulation resulted in the formation of an inner daughter vesicle, “microvesiculation”. By repeating the microvesiculation process, multiple inner GVs could be formed in a single parent semi-vesicle. A semi-vesicle with inner GVs could be detached from the electrode by scraping with a microneedle, yielding an oligovesicular vesicle (OVV) with desired inner aqueous contents. Microvesiculation of a GV held on the tip of a glass micropipette was also possible, and this also produced an OVV. Breaking the membrane of the parent semi-vesicle by micromanipulation with a glass needle after microvesiculation, released the inner GVs. This protocol may be used for controlled formation of GVs with desired contents. Full article
(This article belongs to the Special Issue Biological Membrane Morphogenesis)
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Review

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Open AccessReview Mechanisms of Membrane Curvature Generation in Membrane Traffic
Membranes 2012, 2(1), 118-133; doi:10.3390/membranes2010118
Received: 29 January 2012 / Revised: 20 February 2012 / Accepted: 21 February 2012 / Published: 29 February 2012
Cited by 2 | PDF Full-text (226 KB) | HTML Full-text | XML Full-text
Abstract
During the vesicular trafficking process, cellular membranes undergo dynamic morphological changes, in particular at the vesicle generation and fusion steps. Changes in membrane shape are regulated by small GTPases, coat proteins and other accessory proteins, such as BAR domain-containing proteins. In addition, [...] Read more.
During the vesicular trafficking process, cellular membranes undergo dynamic morphological changes, in particular at the vesicle generation and fusion steps. Changes in membrane shape are regulated by small GTPases, coat proteins and other accessory proteins, such as BAR domain-containing proteins. In addition, membrane deformation entails changes in the lipid composition as well as asymmetric distribution of lipids over the two leaflets of the membrane bilayer. Given that P4-ATPases, which catalyze unidirectional flipping of lipid molecules from the exoplasmic to the cytoplasmic leaflets of the bilayer, are crucial for the trafficking of proteins in the secretory and endocytic pathways, changes in the lipid composition are involved in the vesicular trafficking process. Membrane remodeling is under complex regulation that involves the composition and distribution of lipids as well as assembly of proteins. Full article
(This article belongs to the Special Issue Biological Membrane Morphogenesis)
Open AccessReview The BAR Domain Superfamily Proteins from Subcellular Structures to Human Diseases
Membranes 2012, 2(1), 91-117; doi:10.3390/membranes2010091
Received: 5 January 2012 / Revised: 7 February 2012 / Accepted: 15 February 2012 / Published: 27 February 2012
Cited by 7 | PDF Full-text (369 KB) | HTML Full-text | XML Full-text
Abstract
Eukaryotic cells have complicated membrane systems. The outermost plasma membrane contains various substructures, such as invaginations and protrusions, which are involved in endocytosis and cell migration. Moreover, the intracellular membrane compartments, such as autophagosomes and endosomes, are essential for cellular viability. The [...] Read more.
Eukaryotic cells have complicated membrane systems. The outermost plasma membrane contains various substructures, such as invaginations and protrusions, which are involved in endocytosis and cell migration. Moreover, the intracellular membrane compartments, such as autophagosomes and endosomes, are essential for cellular viability. The Bin-Amphiphysin-Rvs167 (BAR) domain superfamily proteins are important players in membrane remodeling through their structurally determined membrane binding surfaces. A variety of BAR domain superfamily proteins exist, and each family member appears to be involved in the formation of certain subcellular structures or intracellular membrane compartments. Most of the BAR domain superfamily proteins contain SH3 domains, which bind to the membrane scission molecule, dynamin, as well as the actin regulatory WASP/WAVE proteins and several signal transduction molecules, providing possible links between the membrane and the cytoskeleton or other machineries. In this review, we summarize the current information about each BAR superfamily protein with an SH3 domain(s). The involvement of BAR domain superfamily proteins in various diseases is also discussed. Full article
(This article belongs to the Special Issue Biological Membrane Morphogenesis)
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Open AccessReview Membrane Compartment Occupied by Can1 (MCC) and Eisosome Subdomains of the Fungal Plasma Membrane
Membranes 2011, 1(4), 394-411; doi:10.3390/membranes1040394
Received: 31 October 2011 / Revised: 28 November 2011 / Accepted: 5 December 2011 / Published: 13 December 2011
Cited by 14 | PDF Full-text (379 KB) | HTML Full-text | XML Full-text
Abstract
Studies on the budding yeast Saccharomyces cerevisiae have revealed that fungal plasma membranes are organized into different subdomains. One new domain termed MCC/eisosomes consists of stable punctate patches that are distinct from lipid rafts. The MCC/eisosome domains correspond to furrows in the [...] Read more.
Studies on the budding yeast Saccharomyces cerevisiae have revealed that fungal plasma membranes are organized into different subdomains. One new domain termed MCC/eisosomes consists of stable punctate patches that are distinct from lipid rafts. The MCC/eisosome domains correspond to furrows in the plasma membrane that are about 300 nm long and 50 nm deep. The MCC portion includes integral membrane proteins, such as the tetraspanners Sur7 and Nce102. The adjacent eisosome includes proteins that are peripherally associated with the membrane, including the BAR domains proteins Pil1 and Lsp1 that are thought to promote membrane curvature. Genetic analysis of the MCC/eisosome components indicates these domains broadly affect overall plasma membrane organization. The mechanisms regulating the formation of MCC/eisosomes in model organisms will be reviewed as well as the role of these plasma membrane domains in fungal pathogenesis and response to antifungal drugs. Full article
(This article belongs to the Special Issue Biological Membrane Morphogenesis)
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Open AccessReview The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function
Membranes 2011, 1(4), 354-393; doi:10.3390/membranes1040354
Received: 26 October 2011 / Revised: 24 November 2011 / Accepted: 5 December 2011 / Published: 9 December 2011
Cited by 10 | PDF Full-text (576 KB) | HTML Full-text | XML Full-text
Abstract
A large number of RING finger (RNF) proteins are present in eukaryotic cells and the majority of them are believed to act as E3 ubiquitin ligases. In humans, 49 RNF proteins are predicted to contain transmembrane domains, several of which are specifically [...] Read more.
A large number of RING finger (RNF) proteins are present in eukaryotic cells and the majority of them are believed to act as E3 ubiquitin ligases. In humans, 49 RNF proteins are predicted to contain transmembrane domains, several of which are specifically localized to membrane compartments in the secretory and endocytic pathways, as well as to mitochondria and peroxisomes. They are thought to be molecular regulators of the organization and integrity of the functions and dynamic architecture of cellular membrane and membranous organelles. Emerging evidence has suggested that transmembrane RNF proteins control the stability, trafficking and activity of proteins that are involved in many aspects of cellular and physiological processes. This review summarizes the current knowledge of mammalian transmembrane RNF proteins, focusing on their roles and significance. Full article
(This article belongs to the Special Issue Biological Membrane Morphogenesis)

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