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Nuclear Envelope Proteins 2.0
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Nuclear Envelope Proteins 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (31 March 2022) | Viewed by 14645

Special Issue Editor

Dr. James M. Holaska

E-Mail
Guest Editor
Department of Biomedical Sciences, Cooper Medical School of Rowan University, Camden, NJ, USA
Interests: transcriptional regulation; biochemistry; chromatin; cell biology; DNA binding; lamins
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The nuclear envelope functionally separates the nucleoplasm from the cytoplasm. The nuclear envelope is composed of two lipid bilayers—the outer nuclear membrane, which is contiguous with the endoplasmic reticulum, and the inner nuclear membrane. Embedded within the nuclear envelope are the nuclear pore complexes, which provide bi-directional transport across the nuclear membrane. Underlying the inner nuclear membrane is a network of intermediate filament proteins called lamins, which provide the nuclear structure and elasticity.

The outer and inner nuclear membranes are functionally distinct proteinaceous membranes. There are over 100 inner nuclear membrane proteins, many of which are cell type-specific. These proteins have diverse cellular roles, including regulation of nuclear structure, genomic organization, chromatin architecture, gene expression, the cell cycle, and cytoskeletal organization. Given these diverse roles, it is not surprising that mutations in many of these proteins cause or have been linked to many different diseases.

This Special Issue on “Nuclear Envelope Proteins” will contain a selection of research and review articles covering all aspects of nuclear envelope protein structure and function, and will provide mechanistic insight into their function. Studies of nuclear envelope protein function as it relates to disease are also encouraged.

Dr. James M. Holaska
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 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 special issue 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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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.

Keywords

  • Nuclear envelope
  • Lamin
  • Emerin
  • Nuclear membrane
  • Inner nuclear membrane (INM)
  • Nuclear envelope transmembrane protein (NET)
  • LEM (Lap2-emerin-MAN1) domain
  • LINC (linker of nucleoskeleton and cytoskeleton)
  • NPC (nuclear pore complex)
  • Lamina-associated domain (LAD)

Published Papers (4 papers)

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Research

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20 pages, 5550 KiB  
Article
In Silico and In Vivo Analysis of Amino Acid Substitutions That Cause Laminopathies
by Benjamin E. Hinz, Sydney G. Walker, Austin Xiong, Rose A. Gogal, Michael J. Schnieders and Lori L. Wallrath
Int. J. Mol. Sci. 2021, 22(20), 11226; https://doi.org/10.3390/ijms222011226 - 18 Oct 2021
Cited by 6 | Viewed by 2446
Abstract
Mutations in the LMNA gene cause diseases called laminopathies. LMNA encodes lamins A and C, intermediate filaments with multiple roles at the nuclear envelope. LMNA mutations are frequently single base changes that cause diverse disease phenotypes affecting muscles, nerves, and fat. Disease-associated amino [...] Read more.
Mutations in the LMNA gene cause diseases called laminopathies. LMNA encodes lamins A and C, intermediate filaments with multiple roles at the nuclear envelope. LMNA mutations are frequently single base changes that cause diverse disease phenotypes affecting muscles, nerves, and fat. Disease-associated amino acid substitutions were mapped in silico onto three-dimensional structures of lamin A/C, revealing no apparent genotype–phenotype connections. In silico analyses revealed that seven of nine predicted partner protein binding pockets in the Ig-like fold domain correspond to sites of disease-associated amino acid substitutions. Different amino acid substitutions at the same position within lamin A/C cause distinct diseases, raising the question of whether the nature of the amino acid replacement or genetic background differences contribute to disease phenotypes. Substitutions at R249 in the rod domain cause muscular dystrophies with varying severity. To address this variability, we modeled R249Q and R249W in Drosophila Lamin C, an orthologue of LMNA. Larval body wall muscles expressing mutant Lamin C caused abnormal nuclear morphology and premature death. When expressed in indirect flight muscles, R249W caused a greater number of adults with wing posturing defects than R249Q, consistent with observations that R249W and R249Q cause distinct muscular dystrophies, with R249W more severe. In this case, the nature of the amino acid replacement appears to dictate muscle disease severity. Together, our findings illustrate the utility of Drosophila for predicting muscle disease severity and pathogenicity of variants of unknown significance. Full article
(This article belongs to the Special Issue Nuclear Envelope Proteins 2.0)
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18 pages, 3208 KiB  
Article
Regulation of ER Composition and Extent, and Putative Action in Protein Networks by ER/NE Protein TMEM147
by Giannis Maimaris, Andri Christodoulou, Niovi Santama and Carsten Werner Lederer
Int. J. Mol. Sci. 2021, 22(19), 10231; https://doi.org/10.3390/ijms221910231 - 23 Sep 2021
Cited by 4 | Viewed by 2115
Abstract
Nuclear envelope (NE) and endoplasmic reticulum (ER) collaborate to control a multitude of nuclear and cytoplasmic actions. In this context, the transmembrane protein TMEM147 localizes to both NE and ER, and through direct and indirect interactions regulates processes as varied as production and [...] Read more.
Nuclear envelope (NE) and endoplasmic reticulum (ER) collaborate to control a multitude of nuclear and cytoplasmic actions. In this context, the transmembrane protein TMEM147 localizes to both NE and ER, and through direct and indirect interactions regulates processes as varied as production and transport of multipass membrane proteins, neuronal signaling, nuclear-shape, lamina and chromatin dynamics and cholesterol synthesis. Aiming to delineate the emerging multifunctionality of TMEM147 more comprehensively, we set as objectives, first, to assess potentially more fundamental effects of TMEM147 on the ER and, second, to identify significantly TMEM147-associated cell-wide protein networks and pathways. Quantifying curved and flat ER markers RTN4 and CLIMP63/CKAP4, respectively, we found that TMEM147 silencing causes area and intensity increases for both RTN4 and CLIMP63, and the ER in general, with a profound shift toward flat areas, concurrent with reduction in DNA condensation. Protein network and pathway analyses based on comprehensive compilation of TMEM147 interactors, targets and co-factors then served to manifest novel and established roles for TMEM147. Thus, algorithmically simplified significant pathways reflect TMEM147 function in ribosome binding, oxidoreductase activity, G protein-coupled receptor activity and transmembrane transport, while analysis of protein factors and networks identifies hub proteins and corresponding pathways as potential targets of TMEM147 action and of future functional studies. Full article
(This article belongs to the Special Issue Nuclear Envelope Proteins 2.0)
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20 pages, 3438 KiB  
Article
Lamin A/C Is Dispensable to Mechanical Repression of Adipogenesis
by Matthew Goelzer, Amel Dudakovic, Melis Olcum, Buer Sen, Engin Ozcivici, Janet Rubin, Andre J. van Wijnen and Gunes Uzer
Int. J. Mol. Sci. 2021, 22(12), 6580; https://doi.org/10.3390/ijms22126580 - 19 Jun 2021
Cited by 8 | Viewed by 3338
Abstract
Mesenchymal stem cells (MSCs) maintain the musculoskeletal system by differentiating into multiple lineages, including osteoblasts and adipocytes. Mechanical signals, including strain and low-intensity vibration (LIV), are important regulators of MSC differentiation via control exerted through the cell structure. Lamin A/C is a protein [...] Read more.
Mesenchymal stem cells (MSCs) maintain the musculoskeletal system by differentiating into multiple lineages, including osteoblasts and adipocytes. Mechanical signals, including strain and low-intensity vibration (LIV), are important regulators of MSC differentiation via control exerted through the cell structure. Lamin A/C is a protein vital to the nuclear architecture that supports chromatin organization and differentiation and contributes to the mechanical integrity of the nucleus. We investigated whether lamin A/C and mechanoresponsiveness are functionally coupled during adipogenesis in MSCs. siRNA depletion of lamin A/C increased the nuclear area, height, and volume and decreased the circularity and stiffness. Lamin A/C depletion significantly decreased markers of adipogenesis (adiponectin, cellular lipid content) as did LIV treatment despite depletion of lamin A/C. Phosphorylation of focal adhesions in response to mechanical challenge was also preserved during loss of lamin A/C. RNA-seq showed no major adipogenic transcriptome changes resulting from LIV treatment, suggesting that LIV regulation of adipogenesis may not occur at the transcriptional level. We observed that during both lamin A/C depletion and LIV, interferon signaling was downregulated, suggesting potentially shared regulatory mechanism elements that could regulate protein translation. We conclude that the mechanoregulation of adipogenesis and the mechanical activation of focal adhesions function independently from those of lamin A/C. Full article
(This article belongs to the Special Issue Nuclear Envelope Proteins 2.0)
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Review

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29 pages, 3270 KiB  
Review
The Role of Emerin in Cancer Progression and Metastasis
by Alexandra G. Liddane and James M. Holaska
Int. J. Mol. Sci. 2021, 22(20), 11289; https://doi.org/10.3390/ijms222011289 - 19 Oct 2021
Cited by 13 | Viewed by 5825
Abstract
It is commonly recognized in the field that cancer cells exhibit changes in the size and shape of their nuclei. These features often serve as important biomarkers in the diagnosis and prognosis of cancer patients. Nuclear size can significantly impact cell migration due [...] Read more.
It is commonly recognized in the field that cancer cells exhibit changes in the size and shape of their nuclei. These features often serve as important biomarkers in the diagnosis and prognosis of cancer patients. Nuclear size can significantly impact cell migration due to its incredibly large size. Nuclear structural changes are predicted to regulate cancer cell migration. Nuclear abnormalities are common across a vast spectrum of cancer types, regardless of tissue source, mutational spectrum, and signaling dependencies. The pervasiveness of nuclear alterations suggests that changes in nuclear structure may be crucially linked to the transformation process. The factors driving these nuclear abnormalities, and the functional consequences, are not completely understood. Nuclear envelope proteins play an important role in regulating nuclear size and structure in cancer. Altered expression of nuclear lamina proteins, including emerin, is found in many cancers and this expression is correlated with better clinical outcomes. A model is emerging whereby emerin, as well as other nuclear lamina proteins, binding to the nucleoskeleton regulates the nuclear structure to impact metastasis. In this model, emerin and lamins play a central role in metastatic transformation, since decreased emerin expression during transformation causes the nuclear structural defects required for increased cell migration, intravasation, and extravasation. Herein, we discuss the cellular functions of nuclear lamina proteins, with a particular focus on emerin, and how these functions impact cancer progression and metastasis. Full article
(This article belongs to the Special Issue Nuclear Envelope Proteins 2.0)
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