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Article ; Online: Evolution of microRNAs in Amoebozoa and implications for the origin of multicellularity.

Edelbroek, Bart / Kjellin, Jonas / Biryukova, Inna / Liao, Zhen / Lundberg, Torgny / Noegel, Angelika A / Eichinger, Ludwig / Friedländer, Marc R / Söderbom, Fredrik

Nucleic acids research

2024 Volume 52, Issue 6, Page(s) 3121–3136

Abstract: MicroRNAs (miRNAs) are important and ubiquitous regulators of gene expression in both plants and animals. They are thought to have evolved convergently in these lineages and hypothesized to have played a role in the evolution of multicellularity. In line ...

Abstract	MicroRNAs (miRNAs) are important and ubiquitous regulators of gene expression in both plants and animals. They are thought to have evolved convergently in these lineages and hypothesized to have played a role in the evolution of multicellularity. In line with this hypothesis, miRNAs have so far only been described in few unicellular eukaryotes. Here, we investigate the presence and evolution of miRNAs in Amoebozoa, focusing on species belonging to Acanthamoeba, Physarum and dictyostelid taxonomic groups, representing a range of unicellular and multicellular lifestyles. miRNAs that adhere to both the stringent plant and animal miRNA criteria were identified in all examined amoebae, expanding the total number of protists harbouring miRNAs from 7 to 15. We found conserved miRNAs between closely related species, but the majority of species feature only unique miRNAs. This shows rapid gain and/or loss of miRNAs in Amoebozoa, further illustrated by a detailed comparison between two evolutionary closely related dictyostelids. Additionally, loss of miRNAs in the Dictyostelium discoideum drnB mutant did not seem to affect multicellular development and, hence, demonstrates that the presence of miRNAs does not appear to be a strict requirement for the transition from uni- to multicellular life.
MeSH term(s)	Amoebozoa/classification ; Amoebozoa/genetics ; Dictyostelium/genetics ; MicroRNAs/genetics ; Phylogeny ; Evolution, Molecular ; RNA, Protozoan/genetics ; Conserved Sequence/genetics ; RNA Interference
Chemical Substances	MicroRNAs ; RNA, Protozoan
Language	English
Publishing date	2024-02-20
Publishing country	England
Document type	Journal Article
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkae109
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Article ; Online: Functional Analysis of LINC Complexes in the Skin.

Karakesisoglou, Iakowos / Mroß, Carmen / Noegel, Angelika A

Methods in molecular biology (Clifton, N.J.)

2018 Volume 1840, Page(s) 295–306

Abstract: The genome in eukaryotic cells is encased by two intricate and interconnected concentric membranes, which together with the underlying nuclear lamina form the nuclear envelope (NE). Two fundamental macromolecular structures are embedded within the ... ...

Abstract	The genome in eukaryotic cells is encased by two intricate and interconnected concentric membranes, which together with the underlying nuclear lamina form the nuclear envelope (NE). Two fundamental macromolecular structures are embedded within the nuclear envelope: the nuclear pore (NPC) and the LINC complex. The former perforates the nucleus controlling biomolecule trafficking between the nucleoplasm and the cytoplasm, while the latter integrates the nucleus via the cytoskeleton to the extracellular matrix. LINC complex structural and functional integrity is of utmost importance for various fundamental cellular functions. Mechanical forces are relayed into the nuclear interior via the LINC complex, which controls lamina organization, chromosome dynamics, and genome organization and stability. Thus, LINC constituents play pivotal roles in cellular architecture including organelle positioning, cell movement, tissue assembly, organ homeostasis, and organismal aging. The LINC complex oligomeric core contains several multi-isomeric, multifunctional, and often tissue-specific proteins. Therefore, for a proper functional analysis, genetic mouse models are an invaluable resource. Herein, we focus on the LINC complex roles in the skin and describe methods that enable the successful isolation of primary embryonic fibroblast and newborn skin cells, which can be then investigated functionally in vitro.
MeSH term(s)	Animals ; Cell Line ; Cell Movement ; Cell Nucleus/metabolism ; Cells, Cultured ; Cytoskeleton/metabolism ; Fibroblasts/metabolism ; Keratinocytes/metabolism ; Mice ; Multiprotein Complexes/metabolism ; Nuclear Proteins/metabolism ; Skin/metabolism
Chemical Substances	Multiprotein Complexes ; Nuclear Proteins
Language	English
Publishing date	2018-09-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-8691-0_20
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Article ; Online: Inner nuclear envelope protein SUN1 plays a prominent role in mammalian mRNA export.

Li, Ping / Noegel, Angelika A

Nucleic acids research

2015 Volume 43, Issue 20, Page(s) 9874–9888

Abstract: Nuclear export of messenger ribonucleoproteins (mRNPs) through the nuclear pore complex (NPC) can be roughly classified into two forms: bulk and specific export, involving an nuclear RNA export factor 1 (NXF1)-dependent pathway and chromosome region ... ...

Abstract	Nuclear export of messenger ribonucleoproteins (mRNPs) through the nuclear pore complex (NPC) can be roughly classified into two forms: bulk and specific export, involving an nuclear RNA export factor 1 (NXF1)-dependent pathway and chromosome region maintenance 1 (CRM1)-dependent pathway, respectively. SUN proteins constitute the inner nuclear envelope component of the l I: nker of N: ucleoskeleton and C: ytoskeleton (LINC) complex. Here, we show that mammalian cells require SUN1 for efficient nuclear mRNP export. The results indicate that both SUN1 and SUN2 interact with heterogeneous nuclear ribonucleoprotein (hnRNP) F/H and hnRNP K/J. SUN1 depletion inhibits the mRNP export, with accumulations of both hnRNPs and poly(A)+RNA in the nucleus. Leptomycin B treatment indicates that SUN1 functions in mammalian mRNA export involving the NXF1-dependent pathway. SUN1 mediates mRNA export through its association with mRNP complexes via a direct interaction with NXF1. Additionally, SUN1 associates with the NPC through a direct interaction with Nup153, a nuclear pore component involved in mRNA export. Taken together, our results reveal that the inner nuclear envelope protein SUN1 has additional functions aside from being a central component of the LINC complex and that it is an integral component of the mammalian mRNA export pathway suggesting a model whereby SUN1 recruits NXF1-containing mRNP onto the nuclear envelope and hands it over to Nup153.
MeSH term(s)	Cell Nucleus/metabolism ; Cells, Cultured ; HeLa Cells ; Heterogeneous-Nuclear Ribonucleoproteins/metabolism ; Humans ; Membrane Proteins/metabolism ; Membrane Proteins/physiology ; Microtubule-Associated Proteins/metabolism ; Microtubule-Associated Proteins/physiology ; Nuclear Pore Complex Proteins/metabolism ; Nuclear Proteins/metabolism ; Nuclear Proteins/physiology ; RNA Transport ; RNA, Messenger/metabolism ; Repressor Proteins/metabolism
Chemical Substances	Heterogeneous-Nuclear Ribonucleoproteins ; Membrane Proteins ; Microtubule-Associated Proteins ; NFX1 protein, human ; NUP153 protein, human ; Nuclear Pore Complex Proteins ; Nuclear Proteins ; RNA, Messenger ; Repressor Proteins ; SUN1 protein, human
Language	English
Publishing date	2015-11-16
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkv1058
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Book ; Online ; Thesis: Untersuchungen zu phr2AB, einer regulatorischen Untereinheit der Proteinphosphatase PP2A, im Modellorganismus Dictyostelium discoideum

Wehrstedt von Nessen-Lapp, Regina Verfasser] / Noegel, Angelika A. [Verfasser] / Noegel, A. A. [Gutachter] / [Lemberg, Marius [Gutachter]

2022

Author's details	Regina Wehrstedt von Nessen-Lapp, Angelika A. Noegel ; Gutachter: A. A. Noegel, M. K. Lemberg
Keywords	Naturwissenschaften ; Science
Subject code	sg500
Language	German
Publisher	Universitäts- und Stadtbibliothek Köln
Publishing place	Köln
Document type	Book ; Online ; Thesis
Database	Digital theses on the web

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Article: Nesprins in cell stability and migration.

Neumann, Sascha / Noegel, Angelika A

Advances in experimental medicine and biology

2014 Volume 773, Page(s) 491–504

Abstract: Nesprins are a family of proteins that are primarily known for their localization along the nuclear envelope. Together with inner nuclear membrane SUN proteins, they form the core of the LINC (Linker of Nucleoskeleton and Cytoskeleton) complex that ... ...

Abstract	Nesprins are a family of proteins that are primarily known for their localization along the nuclear envelope. Together with inner nuclear membrane SUN proteins, they form the core of the LINC (Linker of Nucleoskeleton and Cytoskeleton) complex that traverses both nuclear membranes to connect the cytoplasm and the nuclear interior. Based on their structure and interactions, Nesprins integrate the nucleus into the cytoskeleton of a cell. Mutations in Nesprins have been identified in a group of human diseases that have been summarized as laminopathies. Cellular functions of the Nesprins and recent studies on different cancer types additionally draw interest on Nesprins in the field of cancer research. Here we summarize recent findings about the structural arrangements of Nesprins along the nuclear envelope, and highlight Nesprin functions in basic cellular processes like maintenance of nuclear shape and size, and of nuclear and cellular or cytoskeletal organization, centrosomal positioning, cell migration, and signal transduction. In summary, Nesprins are involved in critical cellular processes, which in case of malfunction contribute to the formation of cancer and might represent novel targets in cancer diagnosis or for therapeutic intervention.
MeSH term(s)	Cell Movement ; Humans ; Microfilament Proteins/physiology ; Nuclear Envelope/chemistry ; Nuclear Proteins/chemistry ; Organelle Shape ; Signal Transduction
Chemical Substances	Microfilament Proteins ; Nuclear Proteins
Language	English
Publishing date	2014
Publishing country	United States
Document type	Journal Article ; Review
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-1-4899-8032-8_22
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Article: Nesprin-1 impact on tumorigenic cell phenotypes

Sur-Erdem, Ilknur / Hussain, Muhammed Sajid / Asif, Maria / Pınarbası, Nareg / Aksu, Ali Cenk / Noegel, Angelika A

Molecular biology reports. 2020 Feb., v. 47, no. 2

2020

Abstract: The largest protein of the nuclear envelope (NE) is Nesprin-1 which forms a network along the NE interacting with actin, Emerin, Lamin, and SUN proteins. Mutations in the SYNE1 gene and reduction in Nesprin-1 protein levels have been reported to ... ...

Abstract	The largest protein of the nuclear envelope (NE) is Nesprin-1 which forms a network along the NE interacting with actin, Emerin, Lamin, and SUN proteins. Mutations in the SYNE1 gene and reduction in Nesprin-1 protein levels have been reported to correlate with several age related diseases and cancer. In the present study, we tested whether Nesprin-1 overexpression can reverse the malignant phenotype of Huh7 cells, a human liver cancer cell line, which carries a mutation in the SYNE1 gene resulting in reduced Nesprin-1 protein levels, has altered nuclear shape, altered amounts and localization of NE components, centrosome localization and genome stability. Ectopic expression of a mini-Nesprin-1 led to an improvement of the nuclear shape, corrected the mislocalization of NE proteins, the centrosome positioning, and the alterations in the DNA damage response network. Additionally, Nesprin-1 had a profound effect on cellular senescence. These findings suggest that Nesprin-1 may be effective in tumorigenic cell phenotype correction of human liver cancer.
Keywords	DNA damage ; actin ; cell senescence ; centrosomes ; genes ; humans ; liver neoplasms ; molecular biology ; mutation ; neoplasm cells ; nuclear membrane ; phenotype
Language	English
Dates of publication	2020-02
Size	p. 921-934.
Publishing place	Springer Netherlands
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	186544-4
ISSN	1573-4978 ; 0301-4851
ISSN (online)	1573-4978
ISSN	0301-4851
DOI	10.1007/s11033-019-05184-w
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Article ; Online: Comparative genomics in the Amoebozoa clade.

Glöckner, Gernot / Noegel, Angelika A

Biological reviews of the Cambridge Philosophical Society

2013 Volume 88, Issue 1, Page(s) 215–225

Abstract: Amoeboid life forms can be found throughout the evolutionary tree. The greatest proportion of these life forms is found in the Amoebozoa clade, one of the six major eukaryote evolutionary branches. Despite its common origin this clade exhibits a wide ... ...

Abstract	Amoeboid life forms can be found throughout the evolutionary tree. The greatest proportion of these life forms is found in the Amoebozoa clade, one of the six major eukaryote evolutionary branches. Despite its common origin this clade exhibits a wide diversity of lifestyles including free-living and parasitic species and species with multicellular and multinucleate life stages. In this group, development, cooperation, and social behaviour can be studied in addition to traits common to unicellular organisms. To date, only a few Amoebozoa genomes have been sequenced completely, however a number of expressed sequence tags (ESTs) and complete and draft genomes have become available recently for several species that represent some of the major evolutionary lineages in this clade. This resource allows us to compare and analyse the evolutionary history and fate of branch-specific genes if properly exploited. Despite the large evolutionary time scale since the emergence of the major groups the genomic organization in Amoebozoa has retained common features. The number of Amoebozoa-specific genetic inventions seems to be rather small. The emergence of subgroups is accompanied by gene and domain losses and acquisitions of bacterial gene material. The sophisticated developmental cycles of Myxogastria and Dictyosteliida likely have a common origin and are deeply rooted in amoebozoan evolution. In this review we describe initial approaches to comparative genomics in Amoebozoa, summarize recent findings, and identify goals for further studies.
MeSH term(s)	Amoebozoa/genetics ; Animals ; Biological Evolution ; Genome ; Genomics ; Phylogeny
Language	English
Publishing date	2013-02
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1423558-4
ISSN	1469-185X ; 0006-3231 ; 1464-7931
ISSN (online)	1469-185X
ISSN	0006-3231 ; 1464-7931
DOI	10.1111/j.1469-185X.2012.00248.x
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Article ; Online: The role of nesprins as multifunctional organizers in the nucleus and the cytoskeleton.

Noegel, Angelika A / Neumann, Sascha

Biochemical Society transactions

2011 Volume 39, Issue 6, Page(s) 1725–1728

Abstract: Nesprins (nuclear envelope spectrin repeat proteins), also known as SYNE (synaptic nuclear envelope protein), MYNE (myocyte nuclear envelope protein), ENAPTIN and NUANCE, are proteins that are primarily components of the nuclear envelope. The nuclear ... ...

Abstract	Nesprins (nuclear envelope spectrin repeat proteins), also known as SYNE (synaptic nuclear envelope protein), MYNE (myocyte nuclear envelope protein), ENAPTIN and NUANCE, are proteins that are primarily components of the nuclear envelope. The nuclear envelope is a continuous membrane system composed of two lipid bilayers: an inner and an outer nuclear membrane. Nesprins are components of both nuclear membranes and reach into the nucleoplasm and the cytoplasm, where they undergo different interactions and have the potential to influence transcriptional processes and cytoskeletal activities.
MeSH term(s)	Animals ; Cell Nucleus/metabolism ; Cytoskeleton/metabolism ; Disease ; Humans ; Lamins/metabolism ; Membrane Proteins/metabolism ; Protein Binding
Chemical Substances	Lamins ; Membrane Proteins
Language	English
Publishing date	2011-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST20110668
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Article: Nesprin-1 role in DNA damage response

Sur, Ilknur / Neumann, Sascha / Noegel, Angelika A

Nucleus. 2014 Mar. 1, v. 5, no. 2

2014

Abstract: Nuclear envelope (NE) proteins have fundamental roles in maintaining nuclear structure, cell signaling, chromatin organization, and gene regulation, and mutations in genes encoding NE components were identified as primary cause of a number of age ... ...

Abstract	Nuclear envelope (NE) proteins have fundamental roles in maintaining nuclear structure, cell signaling, chromatin organization, and gene regulation, and mutations in genes encoding NE components were identified as primary cause of a number of age associated diseases and cancer. Nesprin-1 belongs to a family of multi-isomeric NE proteins that are characterized by spectrin repeats. We analyzed NE components in various tumor cell lines and found that Nesprin-1 levels were strongly reduced associated with alterations in further NE components. By reducing the amounts of Nesprin-1 by RNAi mediated knockdown, we could reproduce those alterations in mouse and human cell lines. In a search for novel Nesprin-1 binding proteins, we identified MSH2 and MSH6, proteins of the DNA damage response pathway, as interactors and found alterations in the corresponding pathways in cells with lower Nesprin-1 levels. We also noticed increased number of γH2AX foci in the absence of exogenous DNA damage as was seen in tumor cells. The levels of phosphorylated kinases Chk1 and 2 were altered in a manner resembling tumor cells and the levels of Ku70 were low and the protein was not recruited to the DNA after hydroxyurea (HU) treatment. Our findings indicate a role for Nesprin-1 in the DNA damage response pathway and propose Nesprin-1 as novel player in tumorigenesis and genome instability.
Keywords	DNA ; DNA damage ; carcinogenesis ; chromatin ; genes ; genetic instability ; humans ; hydroxyurea ; mice ; neoplasm cells ; neoplasms ; nuclear membrane ; phosphotransferases (kinases) ; spectrin
Language	English
Dates of publication	2014-0301
Size	p. 173-191.
Publishing place	Taylor & Francis
Document type	Article
ZDB-ID	2619626-8
ISSN	1949-1042 ; 1949-1034
ISSN (online)	1949-1042
ISSN	1949-1034
DOI	10.4161/nucl.29023
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Article ; Online: Nesprin-1 role in DNA damage response.

Sur, Ilknur / Neumann, Sascha / Noegel, Angelika A

Nucleus (Austin, Tex.)

2014 Volume 5, Issue 2, Page(s) 173–191

Abstract	Nuclear envelope (NE) proteins have fundamental roles in maintaining nuclear structure, cell signaling, chromatin organization, and gene regulation, and mutations in genes encoding NE components were identified as primary cause of a number of age associated diseases and cancer. Nesprin-1 belongs to a family of multi-isomeric NE proteins that are characterized by spectrin repeats. We analyzed NE components in various tumor cell lines and found that Nesprin-1 levels were strongly reduced associated with alterations in further NE components. By reducing the amounts of Nesprin-1 by RNAi mediated knockdown, we could reproduce those alterations in mouse and human cell lines. In a search for novel Nesprin-1 binding proteins, we identified MSH2 and MSH6, proteins of the DNA damage response pathway, as interactors and found alterations in the corresponding pathways in cells with lower Nesprin-1 levels. We also noticed increased number of γH2AX foci in the absence of exogenous DNA damage as was seen in tumor cells. The levels of phosphorylated kinases Chk1 and 2 were altered in a manner resembling tumor cells and the levels of Ku70 were low and the protein was not recruited to the DNA after hydroxyurea (HU) treatment. Our findings indicate a role for Nesprin-1 in the DNA damage response pathway and propose Nesprin-1 as novel player in tumorigenesis and genome instability.
MeSH term(s)	Animals ; Cell Line, Tumor ; Cell Nucleus Shape ; Centrosome/metabolism ; Cytoskeletal Proteins ; DNA Damage ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation ; Gene Knockdown Techniques ; Humans ; Mice ; MutS Homolog 2 Protein/metabolism ; Nerve Tissue Proteins/deficiency ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Nuclear Envelope/metabolism ; Nuclear Proteins/deficiency ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Protein Isoforms/deficiency ; Protein Isoforms/genetics ; Protein Isoforms/metabolism
Chemical Substances	Cytoskeletal Proteins ; DNA-Binding Proteins ; G-T mismatch-binding protein ; Nerve Tissue Proteins ; Nuclear Proteins ; Protein Isoforms ; SYNE1 protein, human ; Syne1 protein, mouse ; MSH2 protein, human (EC 3.6.1.3) ; MutS Homolog 2 Protein (EC 3.6.1.3)
Language	English
Publishing date	2014-04-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2619626-8
ISSN	1949-1042 ; 1949-1034
ISSN (online)	1949-1042
ISSN	1949-1034
DOI	10.4161/nucl.29023
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