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Article ; Online: Effects of heterologous human tau protein expression in yeast models of proteotoxic stress response.

Zubčić, Klara / Franić, Dina / Pravica, Mihaela / Hof, Patrick R / Šimić, Goran / Boban, Mirta

2023

Abstract: Background: The primary histological characteristic of Alzheimer's disease is the presence of neurofibrillary tangles, which are large aggregates of tau protein. Aging is the primary risk factor for the development of Alzheimer's disease, however, the ... ...

Abstract	Background: The primary histological characteristic of Alzheimer's disease is the presence of neurofibrillary tangles, which are large aggregates of tau protein. Aging is the primary risk factor for the development of Alzheimer's disease, however, the underlying causes of tau protein aggregation and toxicity are unclear. Aims: Here we investigated tau aggregation and toxicity under the conditions of compromised protein homeostasis. Methods: We used heterologous expression of human tau protein in the unicellular eukaryote yeast Saccharomyces cerevisiae with evolutionarily conserved protein quality control pathways and examined tau-dependent toxicity and aggregation using growth assays, fluorescence microscopy, and a split luciferase-based reporter NanoBiT. Results: Tau protein expressed in yeast under mild proteotoxic stress, or in mutants with impaired pathways for proteotoxic stress response, did not lead to synthetic toxicity or the formation of obvious aggregates. Chronologically old cells also did not develop observable tau aggregates. Our examination of tau oligomerization in living cells using NanoBiT reporter suggests that tau does not form significant levels of oligomers under basal conditions or under mild proteotoxic stress. Conclusion: Together our data suggest that human tau protein does not represent a major burden to the protein quality control system in yeast cells.
Language	English
Publishing date	2023-06-21
Publishing country	England
Document type	Journal Article
ZDB-ID	2423461-8
ISSN	1755-5949 ; 1755-5930
ISSN (online)	1755-5949
ISSN	1755-5930
DOI	10.1111/cns.14304
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Article ; Online: Nuclear Ubiquitin-Proteasome Pathways in Proteostasis Maintenance.

Franić, Dina / Zubčić, Klara / Boban, Mirta

Biomolecules

2021 Volume 11, Issue 1

Abstract: Protein homeostasis, or proteostasis, is crucial for the functioning of a cell, as proteins that are mislocalized, present in excessive amounts, or aberrant due to misfolding or other type of damage can be harmful. Proteostasis includes attaining the ... ...

Abstract	Protein homeostasis, or proteostasis, is crucial for the functioning of a cell, as proteins that are mislocalized, present in excessive amounts, or aberrant due to misfolding or other type of damage can be harmful. Proteostasis includes attaining the correct protein structure, localization, and the formation of higher order complexes, and well as the appropriate protein concentrations. Consequences of proteostasis imbalance are evident in a range of neurodegenerative diseases characterized by protein misfolding and aggregation, such as Alzheimer's, Parkinson's, and amyotrophic lateral sclerosis. To protect the cell from the accumulation of aberrant proteins, a network of protein quality control (PQC) pathways identifies the substrates and direct them towards refolding or elimination via regulated protein degradation. The main pathway for degradation of misfolded proteins is the ubiquitin-proteasome system. PQC pathways have been first described in the cytoplasm and the endoplasmic reticulum, however, accumulating evidence indicates that the nucleus is an important PQC compartment for ubiquitination and proteasomal degradation of not only nuclear, but also cytoplasmic proteins. In this review, we summarize the nuclear ubiquitin-proteasome pathways involved in proteostasis maintenance in yeast, focusing on inner nuclear membrane-associated degradation (INMAD) and San1-mediated protein quality control.
MeSH term(s)	Animals ; Cell Nucleus/metabolism ; Humans ; Proteasome Endopeptidase Complex/metabolism ; Protein Folding ; Proteolysis ; Proteostasis ; Ubiquitin/metabolism
Chemical Substances	Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2021-01-04
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom11010054
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Article ; Online: Degradation-mediated protein quality control at the inner nuclear membrane.

Boban, Mirta / Foisner, Roland

Nucleus (Austin, Tex.)

2016 Volume 7, Issue 1, Page(s) 41–49

Abstract: An intricate machinery protects cells from the accumulation of misfolded, non-functional proteins and protein aggregates. Protein quality control pathways have been best described in the cytoplasm and the endoplasmic reticulum, however, recent findings ... ...

Abstract	An intricate machinery protects cells from the accumulation of misfolded, non-functional proteins and protein aggregates. Protein quality control pathways have been best described in the cytoplasm and the endoplasmic reticulum, however, recent findings indicate that the nucleus is also an important compartment for protein quality control. Several nuclear ubiquitinylation pathways target soluble and membrane proteins in the nucleus and mediate their degradation through nuclear proteasomes. In addition, emerging data suggest that nuclear envelope components are also degraded by autophagy, although the mechanisms by which cytoplasmic autophagy machineries get access to nuclear targets remain unclear. In this minireview we summarize the nuclear ubiquitin-proteasome pathways in yeast, focusing on pathways involved in the protein degradation at the inner nuclear membrane. In addition, we discuss potential mechanisms how nuclear targets at the nuclear envelope may be delivered to the cytoplasmic autophagy pathways in yeast and mammals.
MeSH term(s)	Animals ; Autophagy/physiology ; Humans ; Nuclear Envelope/metabolism ; Nuclear Proteins/metabolism ; Protein Aggregates ; Proteolysis ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Nuclear Proteins ; Protein Aggregates ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2016-01-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2619626-8
ISSN	1949-1042 ; 1949-1034
ISSN (online)	1949-1042
ISSN	1949-1034
DOI	10.1080/19491034.2016.1139273
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Article: Degradation-mediated protein quality control at the inner nuclear membrane

Boban, Mirta / Foisner, Roland

Nucleus. 2016 Mar. 1, v. 7, no. 1

2016

Abstract	An intricate machinery protects cells from the accumulation of misfolded, non-functional proteins and protein aggregates. Protein quality control pathways have been best described in the cytoplasm and the endoplasmic reticulum, however, recent findings indicate that the nucleus is also an important compartment for protein quality control. Several nuclear ubiquitinylation pathways target soluble and membrane proteins in the nucleus and mediate their degradation through nuclear proteasomes. In addition, emerging data suggest that nuclear envelope components are also degraded by autophagy, although the mechanisms by which cytoplasmic autophagy machineries get access to nuclear targets remain unclear. In this minireview we summarize the nuclear ubiquitin-proteasome pathways in yeast, focusing on pathways involved in the protein degradation at the inner nuclear membrane. In addition, we discuss potential mechanisms how nuclear targets at the nuclear envelope may be delivered to the cytoplasmic autophagy pathways in yeast and mammals.
Keywords	autophagy ; endoplasmic reticulum ; nuclear membrane ; protein degradation ; protein value ; quality control ; yeasts
Language	English
Dates of publication	2016-0301
Size	p. 41-49.
Publishing place	Taylor & Francis
Document type	Article
ZDB-ID	2619626-8
ISSN	1949-1042 ; 1949-1034
ISSN (online)	1949-1042
ISSN	1949-1034
DOI	10.1080/19491034.2016.1139273
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Article ; Online: Human neuroblastoma SH-SY5Y cells treated with okadaic acid express phosphorylated high molecular weight tau-immunoreactive protein species.

Boban, Mirta / Babić Leko, Mirjana / Miškić, Terezija / Hof, Patrick R / Šimić, Goran

Journal of neuroscience methods

2018 Volume 319, Page(s) 60–68

Abstract: Background: Early stages of Alzheimer's disease (AD) are characterized by high phosphorylation of microtubule-associated protein tau, which may result from the downregulation of protein phosphatases.: New method: In order to model phosphatase ... ...

Abstract	Background: Early stages of Alzheimer's disease (AD) are characterized by high phosphorylation of microtubule-associated protein tau, which may result from the downregulation of protein phosphatases. New method: In order to model phosphatase downregulation and analyze its effect on tau aggregation in vitro, we treated neuroblastoma SH-SY5Y cells with okadaic acid (OA), a protein phosphatase inhibitor, and examined high molecular weight phospho-tau species. Results and comparison with existing methods: OA treatment led to the appearance of heat-stable protein species with apparent molecular weight around 100 kDa, which were immunoreactive to anti-tau antibodies against phosphorylated Ser202 and Ser396. As these high molecular weight tau-immunoreactive proteins (HMW-TIPs) corresponded to the predicted size of two tau monomers, we considered the possibility that they represent phosphorylation-induced tau oligomers. We attempted to dissociate HMW-TIPs by urea and guanidine, as well as by alkaline phosphatase treatment, but HMW-TIPs were stable under all conditions tested. These characteristics resemble properties of certain sodium dodecyl sulfate (SDS)-resistant tau oligomers from AD brains. The absence of HMW-TIPs detection by anti-total tau antibodies Tau46, CP27 and Tau13 may be a consequence of epitope masking and protein truncation. Alternatively, HMW-TIPs may represent previously unreported phosphoproteins cross-reacting with tau. Conclusions: Taken together, our data provide a novel characterization of an OA-based cell culture model in which OA induces the appearance of HMW-TIPs. These findings have implications for further studies of tau under the conditions of protein phosphatase downregulation, aiming to explain mechanisms involved in early events leading to AD.
MeSH term(s)	Alzheimer Disease/enzymology ; Antibodies ; Cell Line, Tumor ; Enzyme Inhibitors/administration & dosage ; Humans ; Models, Biological ; Okadaic Acid/administration & dosage ; Phosphoprotein Phosphatases/antagonists & inhibitors ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Radioimmunoprecipitation Assay ; tau Proteins/immunology ; tau Proteins/metabolism
Chemical Substances	Antibodies ; Enzyme Inhibitors ; MAPT protein, human ; tau Proteins ; Okadaic Acid (1W21G5Q4N2) ; Phosphoprotein Phosphatases (EC 3.1.3.16)
Language	English
Publishing date	2018-09-29
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	282721-9
ISSN	1872-678X ; 0165-0270
ISSN (online)	1872-678X
ISSN	0165-0270
DOI	10.1016/j.jneumeth.2018.09.030
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Article ; Online: Cdc48 and Ubx1 participate in a pathway associated with the inner nuclear membrane that governs Asi1 degradation.

Pantazopoulou, Marina / Boban, Mirta / Foisner, Roland / Ljungdahl, Per O

Journal of cell science

2016 Volume 129, Issue 20, Page(s) 3770–3780

Abstract: The nuclear envelope is a barrier comprising outer and inner membranes that separate the cytoplasm from the nucleoplasm. The two membranes have different physical characteristics and protein compositions. The processes governing the stability of inner ... ...

Abstract	The nuclear envelope is a barrier comprising outer and inner membranes that separate the cytoplasm from the nucleoplasm. The two membranes have different physical characteristics and protein compositions. The processes governing the stability of inner nuclear membrane (INM) proteins are not well characterized. In Saccharomyces cerevisiae, the INM Asi1-Asi3 complex, principally composed of integral membrane proteins Asi1 and Asi3, is an E3 ubiquitin ligase. In addition to its well-documented function in endoplasmic reticulum (ER)-associated degradation, the Doa10 E3 ubiquitin ligase complex partially localizes to the INM. The Asi1-Asi3 and Doa10 complexes define independent INM-associated degradation (INMAD) pathways that target discrete sets of nuclear substrates for proteasomal degradation. Here, we report that Asi1 is rapidly turned over (t
MeSH term(s)	Adenosine Triphosphatases/metabolism ; Cell Cycle Proteins/metabolism ; Cell Nucleus/metabolism ; Endoplasmic Reticulum-Associated Degradation ; Genetic Testing ; Intracellular Signaling Peptides and Proteins/metabolism ; Membrane Proteins/metabolism ; Models, Biological ; Nuclear Envelope/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Proteolysis ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Valosin Containing Protein
Chemical Substances	ASI1 protein, S cerevisiae ; Cell Cycle Proteins ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins ; SHP1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Ubiquitin ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Adenosine Triphosphatases (EC 3.6.1.-) ; CDC48 protein, S cerevisiae (EC 3.6.4.-) ; Valosin Containing Protein (EC 3.6.4.6)
Language	English
Publishing date	2016-08-26
Publishing country	England
Document type	Journal Article
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.189332
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Article ; Online: Atypical ubiquitylation in yeast targets lysine-less Asi2 for proteasomal degradation.

Boban, Mirta / Ljungdahl, Per O / Foisner, Roland

The Journal of biological chemistry

2014 Volume 290, Issue 4, Page(s) 2489–2495

Abstract: Proteins are typically targeted for proteasomal degradation by the attachment of a polyubiquitin chain to ϵ-amino groups of lysine residues. Non-lysine ubiquitylation of proteasomal substrates has been considered an atypical and rare event limited to ... ...

Abstract	Proteins are typically targeted for proteasomal degradation by the attachment of a polyubiquitin chain to ϵ-amino groups of lysine residues. Non-lysine ubiquitylation of proteasomal substrates has been considered an atypical and rare event limited to complex eukaryotes. Here we report that a fully functional lysine-less mutant of an inner nuclear membrane protein in yeast, Asi2, is polyubiquitylated and targeted for proteasomal degradation. Efficient degradation of lysine-free Asi2 requires E3-ligase Doa10 and E2 enzymes Ubc6 and Ubc7, components of the endoplasmic reticulum-associated degradation pathway. Together, our data suggest that non-lysine ubiquitylation may be more prevalent than currently considered.
MeSH term(s)	Cell Nucleus/metabolism ; Cycloheximide/chemistry ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum-Associated Degradation ; Epitopes/chemistry ; Gene Expression Regulation, Fungal ; Lysine/chemistry ; Lysine/genetics ; Membrane Proteins/metabolism ; Mutation ; Plasmids/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Protein Binding ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae Proteins/metabolism ; Ubiquitin/metabolism ; Ubiquitin-Conjugating Enzymes/metabolism ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Asi2 protein, S cerevisiae ; Epitopes ; Membrane Proteins ; Saccharomyces cerevisiae Proteins ; Ubiquitin ; Cycloheximide (98600C0908) ; UBC6 protein, S cerevisiae (EC 2.3.2.23) ; UBC7 protein, S cerevisiae (EC 2.3.2.23) ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; SSM4 protein, S cerevisiae (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2014-12-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M114.600593
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Article: Dal81 enhances Stp1- and Stp2-dependent transcription necessitating negative modulation by inner nuclear membrane protein Asi1 in Saccharomyces cerevisiae.

Boban, Mirta / Ljungdahl, Per O

Genetics

2007 Volume 176, Issue 4, Page(s) 2087–2097

Abstract: The yeast transcription factors Stp1 and Stp2 are synthesized as latent cytoplasmic precursors. In response to extracellular amino acids, the plasma membrane SPS sensor endoproteolytically excises the N-terminal domains that mediate cytoplasmic retention, ...

Abstract	The yeast transcription factors Stp1 and Stp2 are synthesized as latent cytoplasmic precursors. In response to extracellular amino acids, the plasma membrane SPS sensor endoproteolytically excises the N-terminal domains that mediate cytoplasmic retention, enabling the processed forms to efficiently enter the nucleus and induce gene expression. Cytoplasmic retention is not absolute, low levels of full-length Stp1 and Stp2 "leak" into the nucleus, and the concerted action of inner nuclear membrane proteins Asi1, Asi2, and Asi3 restricts their promoter access. In cells lacking Asi function, the precursor forms bind promoters and constitutively induce gene expression. To understand the requirement of Asi-dependent repression, spontaneous mutations in Required for Latent Stp1/2-mediated transcription (RLS) genes that abolish the constitutive expression of SPS sensor-regulated genes in an asi1Delta strain were selected. A single gene, allelic with DAL81, was identified. We show that Dal81 indiscriminately amplifies the transactivation potential of both full-length and processed Stp1 and Stp2 by facilitating promoter binding. In dal81Delta mutants, the repressing activity of the Asi proteins is dispensable, demonstrating that without amplification, the levels of full-length Stp1 and Stp2 that escape cytoplasmic retention are insufficient to activate transcription. Conversely, the high levels of processed Stp1 and Stp2 that accumulate in the nucleus of induced cells activate transcription in the absence of Dal81.
MeSH term(s)	Binding Sites/genetics ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation, Fungal ; Genes, Fungal ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mutation ; Nuclear Envelope/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Promoter Regions, Genetic ; Protein Processing, Post-Translational ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Transcriptional Activation
Chemical Substances	ASI1 protein, S cerevisiae ; DAL81 protein, S cerevisiae ; DNA-Binding Proteins ; Membrane Proteins ; Nuclear Proteins ; RNA-Binding Proteins ; STP1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Stp2 protein, S cerevisiae ; Transcription Factors
Language	English
Publishing date	2007-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2167-2
ISSN	1943-2631 ; 0016-6731
ISSN (online)	1943-2631
ISSN	0016-6731
DOI	10.1534/genetics.107.075077
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Article ; Online: A nuclear ubiquitin-proteasome pathway targets the inner nuclear membrane protein Asi2 for degradation.

Boban, Mirta / Pantazopoulou, Marina / Schick, Anna / Ljungdahl, Per O / Foisner, Roland

Journal of cell science

2014 Volume 127, Issue Pt 16, Page(s) 3603–3613

Abstract: The nuclear envelope consists of inner and outer nuclear membranes. Whereas the outer membrane is an extension of the endoplasmic reticulum, the inner nuclear membrane (INM) represents a unique membranous environment containing specific proteins. The ... ...

Abstract	The nuclear envelope consists of inner and outer nuclear membranes. Whereas the outer membrane is an extension of the endoplasmic reticulum, the inner nuclear membrane (INM) represents a unique membranous environment containing specific proteins. The mechanisms of integral INM protein degradation are unknown. Here, we investigated the turnover of Asi2, an integral INM protein in Saccharomyces cerevisiae. We report that Asi2 is degraded by the proteasome independently of the vacuole and that it exhibited a half-life of ∼45 min. Asi2 exhibits enhanced stability in mutants lacking the E2 ubiquitin conjugating enzymes Ubc6 or Ubc7, or the E3 ubiquitin ligase Doa10. Consistent with these data, Asi2 is post-translationally modified by poly-ubiquitylation in a Ubc7- and Doa10-dependent manner. Importantly Asi2 degradation is significantly reduced in a sts1-2 mutant that fails to accumulate proteasomes in the nucleus, indicating that Asi2 is degraded in the nucleus. Our results reveal a molecular pathway that affects the stability of integral proteins of the inner nuclear membrane and indicate that Asi2 is subject to protein quality control in the nucleus.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Cell Nucleus/enzymology ; Cell Nucleus/genetics ; Cell Nucleus/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Nuclear Envelope/genetics ; Nuclear Envelope/metabolism ; Proteasome Endopeptidase Complex/genetics ; Proteasome Endopeptidase Complex/metabolism ; Proteolysis ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Ubiquitin-Conjugating Enzymes/genetics ; Ubiquitin-Conjugating Enzymes/metabolism ; Ubiquitins/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Asi2 protein, S cerevisiae ; DOA1 protein, S cerevisiae ; Membrane Proteins ; Saccharomyces cerevisiae Proteins ; Ubiquitins ; UBC6 protein, S cerevisiae (EC 2.3.2.23) ; UBC7 protein, S cerevisiae (EC 2.3.2.23) ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2014-06-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.153163
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Article ; Online: Lamins: 'structure goes cycling'.

Boban, Mirta / Braun, Juliane / Foisner, Roland

Biochemical Society transactions

2009 Volume 38, Issue Pt 1, Page(s) 301–306

Abstract: Nuclear intermediate filaments formed by A- and B-type lamins are central components of the nucleoskeleton and are required for the architecture and integrity of the nucleus. There is growing evidence that lamins are also involved in regulatory pathways ... ...

Abstract	Nuclear intermediate filaments formed by A- and B-type lamins are central components of the nucleoskeleton and are required for the architecture and integrity of the nucleus. There is growing evidence that lamins are also involved in regulatory pathways controlling cell proliferation and differentiation. Lamins affect the activity of several transcription factors, such as retinoblastoma protein and c-Fos, and signalling pathways, such as the ERK1/2 (extracellular-signal-regulated kinase 1/2) and Notch pathways, which are key regulators of cell-cycle progression and differentiation. During mitosis, lamins are dynamically reorganized and play active roles in spindle matrix formation and in post-mitotic nuclear reassembly. Several of the cell-cycle-regulating functions of lamins may be impaired in the diseases linked to mutations in lamins and lamin-associated proteins, including striated muscle diseases, lipodystrophies and premature aging syndromes, and contribute to the tissue-specific disease pathologies.
MeSH term(s)	Animals ; Cell Cycle/physiology ; Cell Differentiation/physiology ; Cell Nucleus/metabolism ; Chromatin/metabolism ; DNA Replication ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Gene Order ; Humans ; Intermediate Filaments/metabolism ; Intermediate Filaments/ultrastructure ; Lamins/chemistry ; Lamins/genetics ; Lamins/metabolism ; Proto-Oncogene Proteins c-fos/metabolism ; Retinoblastoma Protein/metabolism ; Signal Transduction/physiology ; Spindle Apparatus/metabolism
Chemical Substances	Chromatin ; Lamins ; Proto-Oncogene Proteins c-fos ; Retinoblastoma Protein ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24)
Language	English
Publishing date	2009-12-31
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST0380301
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