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Article ; Online: Sustained Extracellular Electrical Stimulation Modulates the Permeability of Gap Junctions in

Stürmer, Sophie / Bolz, Sylvia / Zrenner, Eberhart / Ueffing, Marius / Haq, Wadood

International journal of molecular sciences

2024 Volume 25, Issue 3

Abstract: Neurons build vast gap junction-coupled networks (GJ-nets) that are permeable to ions or small molecules, enabling lateral signaling. Herein, we investigate (1) the effect of blinding diseases on GJ-nets in mouse retinas and (2) the impact of electrical ... ...

Abstract	Neurons build vast gap junction-coupled networks (GJ-nets) that are permeable to ions or small molecules, enabling lateral signaling. Herein, we investigate (1) the effect of blinding diseases on GJ-nets in mouse retinas and (2) the impact of electrical stimulation on GJ permeability. GJ permeability was traced in the acute retinal explants of blind retinal degeneration 1 (
MeSH term(s)	Animals ; Mice ; Retinal Degeneration/therapy ; Retinal Degeneration/pathology ; Retina/pathology ; Gap Junctions ; Electric Stimulation ; Permeability
Language	English
Publishing date	2024-01-28
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms25031616
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Article: Paralog-specific TTC30 regulation of Sonic hedgehog signaling.

Hoffmann, Felix / Bolz, Sylvia / Junger, Katrin / Klose, Franziska / Stehle, Isabel F / Ueffing, Marius / Boldt, Karsten / Beyer, Tina

Frontiers in molecular biosciences

2023 Volume 10, Page(s) 1268722

Abstract: The intraflagellar transport (IFT) machinery is essential for cilia assembly, maintenance, and trans-localization of signaling proteins. The IFT machinery consists of two large multiprotein complexes, one of which is the IFT-B. TTC30A and TTC30B are ... ...

Abstract	The intraflagellar transport (IFT) machinery is essential for cilia assembly, maintenance, and trans-localization of signaling proteins. The IFT machinery consists of two large multiprotein complexes, one of which is the IFT-B. TTC30A and TTC30B are integral components of this complex and were previously shown to have redundant functions in the context of IFT, preventing the disruption of IFT-B and, thus, having a severe ciliogenesis defect upon loss of one paralog. In this study, we re-analyzed the paralog-specific protein complexes and discovered a potential involvement of TTC30A or TTC30B in ciliary signaling. Specifically, we investigated a TTC30A-specific interaction with protein kinase A catalytic subunit α, a negative regulator of Sonic hedgehog (Shh) signaling. Defects in this ciliary signaling pathway are often correlated to synpolydactyly, which, intriguingly, is also linked to a rare TTC30 variant. For an in-depth analysis of this unique interaction and the influence on Shh, TTC30A or B single- and double-knockout hTERT-RPE1 were employed, as well as rescue cells harboring wildtype TTC30 or the corresponding mutation. We could show that mutant TTC30A inhibits the ciliary localization of Smoothened. This observed effect is independent of Patched1 but associated with a distinct phosphorylated PKA substrate accumulation upon treatment with forskolin. This rather prominent phenotype was attenuated in mutant TTC30B. Mass spectrometry analysis of wildtype
Language	English
Publishing date	2023-11-23
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2814330-9
ISSN	2296-889X
ISSN	2296-889X
DOI	10.3389/fmolb.2023.1268722
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Article ; Online: Pharmacological Inhibition of the VCP/Proteasome Axis Rescues Photoreceptor Degeneration in RHO

Sen, Merve / Kutsyr, Oksana / Cao, Bowen / Bolz, Sylvia / Arango-Gonzalez, Blanca / Ueffing, Marius

Biomolecules

2021 Volume 11, Issue 10

Abstract: Rhodopsin ( ...

Abstract	Rhodopsin (
MeSH term(s)	Alkaloids/pharmacology ; Animals ; Animals, Genetically Modified ; Benzoquinones/pharmacology ; Disease Models, Animal ; Endoplasmic Reticulum/drug effects ; Endoplasmic Reticulum/genetics ; Humans ; Lactams, Macrocyclic/pharmacology ; Mutation/genetics ; Photoreceptor Cells, Vertebrate/drug effects ; Photoreceptor Cells, Vertebrate/pathology ; Proteasome Endopeptidase Complex/drug effects ; Proteasome Endopeptidase Complex/genetics ; Protein Folding/drug effects ; Proteolysis/drug effects ; Rats ; Retina/drug effects ; Retina/growth & development ; Retina/pathology ; Retinal Degeneration/genetics ; Retinal Degeneration/pathology ; Retinitis Pigmentosa/genetics ; Retinitis Pigmentosa/pathology ; Rhodopsin/genetics ; Rhodopsin/ultrastructure
Chemical Substances	Alkaloids ; Benzoquinones ; Lactams, Macrocyclic ; kifunensine (0NI8960271) ; Rhodopsin (9009-81-8) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; geldanamycin (Z3K3VJ16KU)
Language	English
Publishing date	2021-10-16
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom11101528
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Article ; Online: Feasibility study for a glutamate driven subretinal prosthesis: local subretinal application of glutamate on blind retina evoke network-mediated responses in different types of ganglion cells.

Haq, Wadood / Dietter, Johannes / Bolz, Sylvia / Zrenner, Eberhart

Journal of neural engineering

2018 Volume 15, Issue 4, Page(s) 45004

Abstract: Objective: A feasibility study for a transmitter based subretinal prosthesis, generating visual responses in blind mouse retina is presented.: Approach: Degenerated rd1 mouse retina were stimulated in subretinal configuration by local glutamate (Glu) ...

Abstract	Objective: A feasibility study for a transmitter based subretinal prosthesis, generating visual responses in blind mouse retina is presented. Approach: Degenerated rd1 mouse retina were stimulated in subretinal configuration by local glutamate (Glu) or NMDA application via micropipettes (~1.5 μm) and thereby the outer retinal activity was recorded by calcium-imaging or the ganglion cell (GC) activity was recorded by the multi-electrode array system. The network mediated activation of GC via bipolar cells was approved by the administration of Glu receptor blockers. Main results: Data of the degenerated and blind rd1 mouse retina reveals that the outer retina is Glu sensitive and that the subretinal Glu stimulation promotes network mediated GC responses. Analysis of the spatial activity-spread indicates that the Glu induced cell activation radius in the outer retina (~12.5 μm) and postsynaptically activated GC (~40 μm) is focal to the stimulation pipette tip. Moreover, the application of NMDA in subretinal space also evoked network mediated GC responses. The Glu-activated GC were identified as ON-OFF, OFF and two ON cells types. Significance: This study evaluates the prerequisite for the function of a transmitter based implant, that after the loss of the photoreceptors, the remnant blind retinal network is Glu sensitive and functional, positively. The differential activation of ON (hyperpolarisation) and OFF (depolarisation) bipolar cells by transmitter Glu is a unique feature and of high interest for retinal implants. Therefore, the respective bipolar cell types could only be driven by glutamatergic stimulation accurately and not by electrical stimulation. The preserved functionality of the blind retina at the onset of complete blindness is motivating to continue research on a transmitter-based prosthesis. Since the artificial Glu stimulation mimics the natural retinal input, early implantation of a Glu-prosthesis might delay the devastating retinal remodelling positively, due to the neuronal-plasticity.
MeSH term(s)	Animals ; Blindness/physiopathology ; Blindness/therapy ; Electric Stimulation/methods ; Evoked Potentials, Visual/drug effects ; Evoked Potentials, Visual/physiology ; Feasibility Studies ; Glutamic Acid/administration & dosage ; Mice ; Mice, Transgenic ; Nerve Net/drug effects ; Nerve Net/physiology ; Organ Culture Techniques ; Photic Stimulation/methods ; Retina/drug effects ; Retina/physiology ; Retinal Ganglion Cells/drug effects ; Retinal Ganglion Cells/physiology ; Retinitis Pigmentosa/physiopathology ; Retinitis Pigmentosa/therapy ; Visual Prosthesis
Chemical Substances	Glutamic Acid (3KX376GY7L)
Language	English
Publishing date	2018-06-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2170901-4
ISSN	1741-2552 ; 1741-2560
ISSN (online)	1741-2552
ISSN	1741-2560
DOI	10.1088/1741-2552/aac811
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Article ; Online: TTC30A and TTC30B Redundancy Protects IFT Complex B Integrity and Its Pivotal Role in Ciliogenesis.

Hoffmann, Felix / Bolz, Sylvia / Junger, Katrin / Klose, Franziska / Schubert, Timm / Woerz, Franziska / Boldt, Karsten / Ueffing, Marius / Beyer, Tina

Genes

2022 Volume 13, Issue 7

Abstract: Intraflagellar transport (IFT) is a microtubule-based system that supports the assembly and maintenance of cilia. The dysfunction of IFT leads to ciliopathies of variable severity. Two of the IFT-B components are the paralogue proteins TTC30A and TTC30B. ...

Abstract	Intraflagellar transport (IFT) is a microtubule-based system that supports the assembly and maintenance of cilia. The dysfunction of IFT leads to ciliopathies of variable severity. Two of the IFT-B components are the paralogue proteins TTC30A and TTC30B. To investigate whether these proteins constitute redundant functions, CRISPR/Cas9 was used to generate single TTC30A or B and double-knockout hTERT-RPE1 cells. Ciliogenesis assays showed the redundancy of both proteins while the polyglutamylation of cilia was affected in single knockouts. The localization of other IFT components was not affected by the depletion of a single paralogue. A loss of both proteins led to a severe ciliogenesis defect, resulting in no cilia formation, which was rescued by TTC30A or B. The redundancy can be explained by the highly similar interaction patterns of the paralogues; both equally interact with the IFT-B machinery. Our study demonstrates that a loss of one TTC30 paralogue can mostly be compensated by the other, thus preventing severe ciliary defects. However, cells assemble shorter cilia, which are potentially limited in their function, especially because of impaired polyglutamylation. A complete loss of both proteins leads to a deficit in IFT complex B integrity followed by disrupted IFT and subsequently no cilia formation.
MeSH term(s)	Biological Transport ; Cilia/genetics ; Cilia/metabolism ; Ciliopathies/genetics ; Ciliopathies/metabolism ; Humans ; Proteins/metabolism
Chemical Substances	Proteins
Language	English
Publishing date	2022-07-01
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2527218-4
ISSN	2073-4425 ; 2073-4425
ISSN (online)	2073-4425
ISSN	2073-4425
DOI	10.3390/genes13071191
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Article ; Online: Interactome Analysis Reveals a Link of the Novel ALMS1-CEP70 Complex to Centrosomal Clusters.

Woerz, Franziska / Hoffmann, Felix / Antony, Shibu / Bolz, Sylvia / Jarboui, Mohamed Ali / Junger, Katrin / Klose, Franziska / Stehle, Isabel F / Boldt, Karsten / Ueffing, Marius / Beyer, Tina

Molecular & cellular proteomics : MCP

2023 Volume 23, Issue 1, Page(s) 100701

Abstract: Alström syndrome (ALMS) is a very rare autosomal-recessive disorder, causing a broad range of clinical defects most notably retinal degeneration, type 2 diabetes, and truncal obesity. The ALMS1 gene encodes a complex and huge ∼0.5 MDa protein, which has ... ...

Abstract	Alström syndrome (ALMS) is a very rare autosomal-recessive disorder, causing a broad range of clinical defects most notably retinal degeneration, type 2 diabetes, and truncal obesity. The ALMS1 gene encodes a complex and huge ∼0.5 MDa protein, which has hampered analysis in the past. The ALMS1 protein is localized to the centrioles and the basal body of cilia and is involved in signaling processes, for example, TGF-β signaling. However, the exact molecular function of ALMS1 at the basal body remains elusive and controversial. We recently demonstrated that protein complex analysis utilizing endogenously tagged cells provides an excellent tool to investigate protein interactions of ciliary proteins. Here, CRISPR/Cas9-mediated endogenously tagged ALMS1 cells were used for affinity-based protein complex analysis. Centrosomal and microtubule-associated proteins were identified, which are potential regulators of ALMS1 function, such as the centrosomal protein 70 kDa (CEP70). Candidate proteins were further investigated in ALMS1-deficient hTERT-RPE1 cells. Loss of ALMS1 led to shortened cilia with no change in structural protein localization, for example, acetylated and ɣ-tubulin, Centrin-3, or the novel interactor CEP70. Conversely, reduction of CEP70 resulted in decreased ALMS1 at the ciliary basal body. Complex analysis of CEP70 revealed domain-specific ALMS1 interaction involving the TPR-containing C-terminal (TRP-CT) fragment of CEP70. In addition to ALMS1, several ciliary proteins, including CEP135, were found to specifically bind to the TPR-CT domain. Data are available via ProteomeXchange with the identifier PXD046401. Protein interactors identified in this study provide candidate lists that help to understand ALMS1 and CEP70 function in cilia-related protein modification, cell death, and disease-related mechanisms.
MeSH term(s)	Humans ; Alstrom Syndrome/genetics ; Alstrom Syndrome/metabolism ; Cell Cycle Proteins/genetics ; Diabetes Mellitus, Type 2 ; Microtubule-Associated Proteins/metabolism ; Obesity ; Tubulin
Chemical Substances	ALMS1 protein, human ; Cell Cycle Proteins ; Microtubule-Associated Proteins ; Tubulin ; CEP70 protein, human
Language	English
Publishing date	2023-12-18
Publishing country	United States
Document type	Journal Article
ZDB-ID	2075924-1
ISSN	1535-9484 ; 1535-9476
ISSN (online)	1535-9484
ISSN	1535-9476
DOI	10.1016/j.mcpro.2023.100701
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Article ; Online: Loss of Complement Factor H impairs antioxidant capacity and energy metabolism of human RPE cells.

Armento, Angela / Honisch, Sabina / Panagiotakopoulou, Vasiliki / Sonntag, Inga / Jacob, Anke / Bolz, Sylvia / Kilger, Ellen / Deleidi, Michela / Clark, Simon / Ueffing, Marius

Scientific reports

2020 Volume 10, Issue 1, Page(s) 10320

Abstract: Polymorphisms in the Complement Factor H (CFH) gene, coding for the Factor H protein (FH), can increase the risk for age-related macular degeneration (AMD). AMD-associated CFH risk variants, Y402H in particular, impair FH function leading to complement ... ...

Abstract	Polymorphisms in the Complement Factor H (CFH) gene, coding for the Factor H protein (FH), can increase the risk for age-related macular degeneration (AMD). AMD-associated CFH risk variants, Y402H in particular, impair FH function leading to complement overactivation. Whether this alone suffices to trigger AMD pathogenesis remains unclear. In AMD, retinal homeostasis is compromised due to the dysfunction of retinal pigment epithelium (RPE) cells. To investigate the impact of endogenous FH loss on RPE cell balance, we silenced CFH in human hTERT-RPE1 cells. FH reduction led to accumulation of C3, at both RNA and protein level and increased RPE vulnerability toward oxidative stress. Mild hydrogen-peroxide exposure in combination with CFH knock-down led to a reduction of glycolysis and mitochondrial respiration, paralleled by an increase in lipid peroxidation, which is a key aspect of AMD pathogenesis. In parallel, cell viability was decreased. The perturbations of energy metabolism were accompanied by transcriptional deregulation of several glucose metabolism genes as well as genes modulating mitochondrial stability. Our data suggest that endogenously produced FH contributes to transcriptional and metabolic homeostasis and protects RPE cells from oxidative stress, highlighting a novel role of FH in AMD pathogenesis.
MeSH term(s)	Cell Line ; Cell Survival/genetics ; Complement Factor H/deficiency ; Complement Factor H/genetics ; Energy Metabolism/genetics ; Epithelial Cells/pathology ; Gene Knockdown Techniques ; Glycolysis/genetics ; Humans ; Lipid Peroxidation/genetics ; Macular Degeneration/genetics ; Macular Degeneration/pathology ; Oxidative Stress/genetics ; Retinal Pigment Epithelium/cytology ; Retinal Pigment Epithelium/pathology
Chemical Substances	CFH protein, human ; Complement Factor H (80295-65-4)
Language	English
Publishing date	2020-06-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-020-67292-z
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Article: Pharmacokinetics of Pullulan-Dexamethasone Conjugates in Retinal Drug Delivery.

Kicková, Eva / Sadeghi, Amir / Puranen, Jooseppi / Tavakoli, Shirin / Sen, Merve / Ranta, Veli-Pekka / Arango-Gonzalez, Blanca / Bolz, Sylvia / Ueffing, Marius / Salmaso, Stefano / Caliceti, Paolo / Toropainen, Elisa / Ruponen, Marika / Urtti, Arto

Pharmaceutics

2021 Volume 14, Issue 1

Abstract: The treatment of retinal diseases by intravitreal injections requires frequent administration unless drug delivery systems with long retention and controlled release are used. In this work, we focused on pullulan (≈67 kDa) conjugates of dexamethasone as ... ...

Abstract	The treatment of retinal diseases by intravitreal injections requires frequent administration unless drug delivery systems with long retention and controlled release are used. In this work, we focused on pullulan (≈67 kDa) conjugates of dexamethasone as therapeutic systems for intravitreal administration. The pullulan-dexamethasone conjugates self-assemble into negatively charged nanoparticles (average size 326 ± 29 nm). Intravitreal injections of pullulan and pullulan-dexamethasone were safe in mouse, rat and rabbit eyes. Fluorescently labeled pullulan particles showed prolonged retention in the vitreous and they were almost completely eliminated via aqueous humor outflow. Pullulan conjugates also distributed to the retina via Müller glial cells when tested in ex vivo retina explants and in vivo. Pharmacokinetic simulations showed that pullulan-dexamethasone conjugates may release free and active dexamethasone in the vitreous humor for over 16 days, even though a large fraction of dexamethasone may be eliminated from the eye as bound pullulan-dexamethasone. We conclude that pullulan based drug conjugates are promising intravitreal drug delivery systems as they may reduce injection frequency and deliver drugs into the retinal cells.
Language	English
Publishing date	2021-12-21
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2527217-2
ISSN	1999-4923
ISSN	1999-4923
DOI	10.3390/pharmaceutics14010012
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Article: Expression of poly(ADP-ribose) glycohydrolase in wild-type and PARG-110 knock-out retina.

Sahaboglu, Ayse / Bolz, Sylvia / Löwenheim, Hubert / Paquet-Durand, Francois

Advances in experimental medicine and biology

2014 Volume 801, Page(s) 463–469

Abstract: Poly(ADP-ribose) (PAR) turnover is required for many cellular processes, and highly relevant for cell death and survival. This post-translational protein modification is regulated by the synthesizing enzyme poly(ADP)ribose-polymerase (PARP) and the ... ...

Abstract	Poly(ADP-ribose) (PAR) turnover is required for many cellular processes, and highly relevant for cell death and survival. This post-translational protein modification is regulated by the synthesizing enzyme poly(ADP)ribose-polymerase (PARP) and the degrading enzyme poly(ADP-ribose) glycohydrolase (PARG). Previously, PARP activity was found to be involved in photoreceptor degeneration in the rd1 mouse and in rd1-like conditions PARP-1 was the main PARP family member contributing to photoreceptor cell death. Despite the manifest role of PARP and PAR accumulation in photoreceptor cell death, the influence of PAR degradation on photoreceptor viability was still unknown. Here, we investigated the role of PARG in photoreceptor degeneration using the PARG-110 knock out mouse and report for the first time on PARG expression in wild-type and knock-out retina.
MeSH term(s)	Animals ; Disease Models, Animal ; Enzyme Inhibitors/pharmacology ; Glycoside Hydrolases/antagonists & inhibitors ; Glycoside Hydrolases/genetics ; Glycoside Hydrolases/metabolism ; Mice ; Mice, Knockout ; Neuroprotective Agents/pharmacology ; Photoreceptor Cells, Vertebrate/drug effects ; Photoreceptor Cells, Vertebrate/pathology ; Photoreceptor Cells, Vertebrate/physiology ; Poly (ADP-Ribose) Polymerase-1 ; Poly(ADP-ribose) Polymerases/genetics ; Poly(ADP-ribose) Polymerases/metabolism ; Retina/drug effects ; Retina/pathology ; Retina/physiology ; Retinal Degeneration/genetics ; Retinal Degeneration/metabolism ; Retinal Degeneration/physiopathology
Chemical Substances	Enzyme Inhibitors ; Neuroprotective Agents ; Parp1 protein, mouse (EC 2.4.2.30) ; Poly (ADP-Ribose) Polymerase-1 (EC 2.4.2.30) ; Poly(ADP-ribose) Polymerases (EC 2.4.2.30) ; Glycoside Hydrolases (EC 3.2.1.-) ; poly ADP-ribose glycohydrolase (EC 3.2.1.143)
Language	English
Publishing date	2014
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-1-4614-3209-8_59
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Article ; Online: CRISPR/Cas9-mediated Genomic Editing of Cluap1/IFT38 Reveals a New Role in Actin Arrangement.

Beyer, Tina / Bolz, Sylvia / Junger, Katrin / Horn, Nicola / Moniruzzaman, Muhammad / Wissinger, Yasmin / Ueffing, Marius / Boldt, Karsten

Molecular & cellular proteomics : MCP

2018 Volume 17, Issue 7, Page(s) 1285–1294

Abstract: CRISPR/Cas9-mediated gene editing allows manipulation of a gene of interest in its own chromosomal context. When applied to the analysis of protein interactions and in contrast to exogenous expression of a protein, this can be studied maintaining ... ...

Abstract	CRISPR/Cas9-mediated gene editing allows manipulation of a gene of interest in its own chromosomal context. When applied to the analysis of protein interactions and in contrast to exogenous expression of a protein, this can be studied maintaining physiological stoichiometry, topology, and context. We have used CRISPR/Cas9-mediated genomic editing to investigate Cluap1/IFT38, a component of the intraflagellar transport complex B (IFT-B). Cluap1 has been implicated in human development as well as in cancer progression. Cluap1 loss of function results in early developmental defects with neural tube closure, sonic hedgehog signaling and left-right defects. Herein, we generated an endogenously tagged Cluap1 for protein complex analysis, which was then correlated to the corresponding interactome determined by ectopic expression. Besides IFT-B complex components, new interacting proteins like Ephrin-B1 and TRIP6, which are known to be involved in cytoskeletal arrangement and protein transport, were identified. With the identification of platelet-derived growth factor A (PDGFA) and coiled-coil domain-containing protein 6 (CCDC6) two new interactions were discovered, which link Cluap1 to ciliogenesis and cancer development. The CRISPR/Cas9-mediated knockout of Cluap1 revealed a new phenotype affecting the actin cytoskeleton. Together, these data provide first evidence for a role of Cluap1 not only for cilia assembly and maintenance but also for cytoskeletal rearrangement and intracellular transport processes.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Actins/metabolism ; Antigens, Neoplasm/metabolism ; CRISPR-Associated Protein 9/metabolism ; CRISPR-Cas Systems/genetics ; Cell Movement ; Cilia/metabolism ; Gene Editing ; HEK293 Cells ; Humans ; Protein Isoforms/metabolism ; Telomerase/metabolism
Chemical Substances	Actins ; Antigens, Neoplasm ; CLUAP1 protein, human ; Protein Isoforms ; Telomerase (EC 2.7.7.49) ; CRISPR-Associated Protein 9 (EC 3.1.-)
Language	English
Publishing date	2018-04-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2075924-1
ISSN	1535-9484 ; 1535-9476
ISSN (online)	1535-9484
ISSN	1535-9476
DOI	10.1074/mcp.RA117.000487
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