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Nuclear Envelope Proteins
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Nuclear Envelope Proteins

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

Deadline for manuscript submissions: closed (30 June 2019) | Viewed by 14546

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 named lamins, which provide 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 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 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 (3 papers)

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Research

13 pages, 7175 KiB  
Article
Nucleoplasmic Reticulum Formation in Human Endometrial Cells is Steroid Hormone Responsive and Recruits Nascent Components
by Lior Pytowski, Marek M. Drozdz, Haibo Jiang, Zayra Hernandez, Kurun Kumar, Emily Knott and David J. Vaux
Int. J. Mol. Sci. 2019, 20(23), 5839; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20235839 - 20 Nov 2019
Cited by 6 | Viewed by 3403
Abstract
The nuclei of cells may exhibit invaginations of the nuclear envelope under a variety of conditions. These invaginations form a branched network termed the nucleoplasmic reticulum (NR), which may be found in cells in pathological and physiological conditions. While an extensive NR is [...] Read more.
The nuclei of cells may exhibit invaginations of the nuclear envelope under a variety of conditions. These invaginations form a branched network termed the nucleoplasmic reticulum (NR), which may be found in cells in pathological and physiological conditions. While an extensive NR is a hallmark of cellular senescence and shows associations with some cancers, very little is known about the formation of NR in physiological conditions, despite the presence of extensive nuclear invaginations in some cell types such as endometrial cells. Here we show that in these cells the NR is formed in response to reproductive hormones. We demonstrate that oestrogen and progesterone are sufficient to induce NR formation and that this process is reversible without cell division upon removal of the hormonal stimulus. Nascent lamins and phospholipids are incorporated into the invaginations suggesting that there is a dedicated machinery for its formation. The induction of NR in endometrial cells offers a new model to study NR formation and function in physiological conditions. Full article
(This article belongs to the Special Issue Nuclear Envelope Proteins)
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19 pages, 2980 KiB  
Article
Quantification of the Lamin A/C Transcript Variants in Cancer Cell Lines by Targeted Absolute Quantitative Proteomics and Correlation with mRNA Expression
by Wedad Saeed Al-Qahtani, Mai Abduljabbar, Entissar S. AlSuhaibani, Anas Abdel Rahman and Ahmad Aljada
Int. J. Mol. Sci. 2019, 20(8), 1902; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20081902 - 17 Apr 2019
Cited by 9 | Viewed by 5340
Abstract
Lamin A/C proteins have key roles in nuclear structural integrity and chromosomal stability. Lamin A/C cumulative protein expression of all variants is reported by semi-quantitative Western blotting. To date, there have not been specific antibodies for the individual Lamin A/C transcript variants. We [...] Read more.
Lamin A/C proteins have key roles in nuclear structural integrity and chromosomal stability. Lamin A/C cumulative protein expression of all variants is reported by semi-quantitative Western blotting. To date, there have not been specific antibodies for the individual Lamin A/C transcript variants. We developed a mass spectrometric approach for the quantification of Lamin A/C transcript variants. A signature peptide for each specific splice variant of Lamin A/C was selected. A LC–MS/MS assay based on the selected signature peptides and their labeled internal standards was established to measure the expression of Lamin A/C transcript variant concentrations. The method validation was carried out according to Food and Drug Administration (FDA) guidelines. The expression levels of the Lamin A/C transcript variants were measured in samples derived from MCF7 and U937 cell lines. RT-qPCR assay was also used to quantitate and compare the mRNA expression of splice variants of Lamin A/C. The established and validated method showed a great linearity, sensitivity, and precision. The different expressed Lamin A/C variants in different cell lines were measured and their levels were in concordance with qRT-PCR results. The developed method is reproducible, reliable, and sensitive for measuring different Lamin A/C transcript variants in different cell lines. Full article
(This article belongs to the Special Issue Nuclear Envelope Proteins)
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19 pages, 5372 KiB  
Article
Targeting of LRRC59 to the Endoplasmic Reticulum and the Inner Nuclear Membrane
by Marina Blenski and Ralph H. Kehlenbach
Int. J. Mol. Sci. 2019, 20(2), 334; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20020334 - 15 Jan 2019
Cited by 14 | Viewed by 5227
Abstract
LRRC59 (leucine-rich repeat-containing protein 59) is a tail-anchored protein with a single transmembrane domain close to its C-terminal end that localizes to the endoplasmic reticulum (ER) and the nuclear envelope. Here, we investigate the mechanisms of membrane integration of LRRC59 and its targeting [...] Read more.
LRRC59 (leucine-rich repeat-containing protein 59) is a tail-anchored protein with a single transmembrane domain close to its C-terminal end that localizes to the endoplasmic reticulum (ER) and the nuclear envelope. Here, we investigate the mechanisms of membrane integration of LRRC59 and its targeting to the inner nuclear membrane (INM). Using purified microsomes, we show that LRRC59 can be post-translationally inserted into ER-derived membranes. The TRC-pathway, a major route for post-translational membrane insertion, is not required for LRRC59. Like emerin, another tail-anchored protein, LRRC59 reaches the INM, as demonstrated by rapamycin-dependent dimerization assays. Using different approaches to inhibit importin α/β-dependent nuclear import of soluble proteins, we show that the classic nuclear transport machinery does not play a major role in INM-targeting of LRRC59. Instead, the size of the cytoplasmic domain of LRRC59 is an important feature, suggesting that targeting is governed by passive diffusion. Full article
(This article belongs to the Special Issue Nuclear Envelope Proteins)
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