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Article ; Online: Endogenous Tagging of Ciliary Genes in Human RPE1 Cells for Live-Cell Imaging.

Kuhns, Stefanie / Juhl, Alice Dupont / Anvarian, Zeinab / Wüstner, Daniel / Pedersen, Lotte B / Andersen, Jens S

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

2023 Volume 2725, Page(s) 147–166

Abstract: CRISPR-mediated endogenous tagging of genes provides unique possibilities to explore the function and dynamic subcellular localization of proteins in living cells. Here, we describe experimental strategies for endogenous PCR-tagging of ciliary genes in ... ...

Abstract	CRISPR-mediated endogenous tagging of genes provides unique possibilities to explore the function and dynamic subcellular localization of proteins in living cells. Here, we describe experimental strategies for endogenous PCR-tagging of ciliary genes in human RPE1 cells and how image acquisition and analysis of the expressed fluorescently tagged proteins can be utilized to study the dynamic ciliary processes of intraflagellar transport and vesicular trafficking.
MeSH term(s)	Humans ; Protein Transport/genetics ; Cilia/metabolism ; Proteins/metabolism ; Biological Transport
Chemical Substances	Proteins
Language	English
Publishing date	2023-10-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-3507-0_9
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Article ; Online: Transient accumulation and bidirectional movement of KIF13B in primary cilia.

Juhl, Alice Dupont / Anvarian, Zeinab / Kuhns, Stefanie / Berges, Julia / Andersen, Jens S / Wüstner, Daniel / Pedersen, Lotte B

Journal of cell science

2022 Volume 136, Issue 5

Abstract: Primary cilia are microtubule-based sensory organelles whose assembly and function rely on the conserved bidirectional intraflagellar transport (IFT) system, which is powered by anterograde kinesin-2 and retrograde cytoplasmic dynein-2 motors. Nematodes ... ...

Abstract	Primary cilia are microtubule-based sensory organelles whose assembly and function rely on the conserved bidirectional intraflagellar transport (IFT) system, which is powered by anterograde kinesin-2 and retrograde cytoplasmic dynein-2 motors. Nematodes additionally employ a cell-type-specific kinesin-3 motor, KLP-6, which moves within cilia independently of IFT and regulates ciliary content and function. Here, we provide evidence that a KLP-6 homolog, KIF13B, undergoes bursts of bidirectional movement within primary cilia of cultured immortalized human retinal pigment epithelial (hTERT-RPE1) cells. Anterograde and retrograde intraciliary velocities of KIF13B were similar to those of IFT (as assayed using IFT172-eGFP), but intraciliary movement of KIF13B required its own motor domain and appeared to be cell-type specific. Our work provides the first demonstration of motor-driven, intraciliary movement by a vertebrate kinesin other than kinesin-2 motors.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Biological Transport ; Cilia/metabolism ; Cytoskeletal Proteins/metabolism ; Flagella/metabolism ; Humans ; Kinesins/genetics ; Microtubules
Chemical Substances	Adaptor Proteins, Signal Transducing ; Cytoskeletal Proteins ; IFT172 protein, human ; KIF13B protein, human (EC 3.6.1.-) ; Kinesins (EC 3.6.4.4)
Language	English
Publishing date	2022-05-17
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.259257
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Article: A targeted multi-proteomics approach generates a blueprint of the ciliary ubiquitinome.

Aslanyan, Mariam G / Doornbos, Cenna / Diwan, Gaurav D / Anvarian, Zeinab / Beyer, Tina / Junger, Katrin / van Beersum, Sylvia E C / Russell, Robert B / Ueffing, Marius / Ludwig, Alexander / Boldt, Karsten / Pedersen, Lotte B / Roepman, Ronald

Frontiers in cell and developmental biology

2023 Volume 11, Page(s) 1113656

Abstract: Establishment and maintenance of the primary cilium as a signaling-competent organelle requires a high degree of fine tuning, which is at least in part achieved by a variety of post-translational modifications. One such modification is ubiquitination. ... ...

Abstract	Establishment and maintenance of the primary cilium as a signaling-competent organelle requires a high degree of fine tuning, which is at least in part achieved by a variety of post-translational modifications. One such modification is ubiquitination. The small and highly conserved ubiquitin protein possesses a unique versatility in regulating protein function
Language	English
Publishing date	2023-01-26
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2023.1113656
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Article ; Online: Cellular signalling by primary cilia in development, organ function and disease.

Anvarian, Zeinab / Mykytyn, Kirk / Mukhopadhyay, Saikat / Pedersen, Lotte Bang / Christensen, Søren Tvorup

Nature reviews. Nephrology

2019 Volume 15, Issue 4, Page(s) 199–219

Abstract: Primary cilia project in a single copy from the surface of most vertebrate cell types; they detect and transmit extracellular cues to regulate diverse cellular processes during development and to maintain tissue homeostasis. The sensory capacity of ... ...

Abstract	Primary cilia project in a single copy from the surface of most vertebrate cell types; they detect and transmit extracellular cues to regulate diverse cellular processes during development and to maintain tissue homeostasis. The sensory capacity of primary cilia relies on the coordinated trafficking and temporal localization of specific receptors and associated signal transduction modules in the cilium. The canonical Hedgehog (HH) pathway, for example, is a bona fide ciliary signalling system that regulates cell fate and self-renewal in development and tissue homeostasis. Specific receptors and associated signal transduction proteins can also localize to primary cilia in a cell type-dependent manner; available evidence suggests that the ciliary constellation of these proteins can temporally change to allow the cell to adapt to specific developmental and homeostatic cues. Consistent with important roles for primary cilia in signalling, mutations that lead to their dysfunction underlie a pleiotropic group of diseases and syndromic disorders termed ciliopathies, which affect many different tissues and organs of the body. In this Review, we highlight central mechanisms by which primary cilia coordinate HH, G protein-coupled receptor, WNT, receptor tyrosine kinase and transforming growth factor-β (TGFβ)/bone morphogenetic protein (BMP) signalling and illustrate how defects in the balanced output of ciliary signalling events are coupled to developmental disorders and disease progression.
MeSH term(s)	Cell Differentiation ; Cell Movement ; Cilia/metabolism ; Cilia/pathology ; Ciliary Motility Disorders/metabolism ; Ciliary Motility Disorders/pathology ; Hedgehog Proteins/metabolism ; Homeostasis ; Humans ; Organogenesis ; Signal Transduction
Chemical Substances	Hedgehog Proteins
Language	English
Publishing date	2019-02-01
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2490366-8
ISSN	1759-507X ; 1759-5061
ISSN (online)	1759-507X
ISSN	1759-5061
DOI	10.1038/s41581-019-0116-9
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Article: DLG1 functions upstream of SDCCAG3 and IFT20 to control ciliary targeting of polycystin-2.

bioRxiv : the preprint server for biology

2024

Abstract: Polarized vesicular trafficking directs specific receptors and ion channels to cilia, but the underlying mechanisms are poorly understood. Here we describe a role for DLG1, a core component of the Scribble polarity complex, in regulating ciliary protein ... ...

Abstract	Polarized vesicular trafficking directs specific receptors and ion channels to cilia, but the underlying mechanisms are poorly understood. Here we describe a role for DLG1, a core component of the Scribble polarity complex, in regulating ciliary protein trafficking in kidney epithelial cells. Conditional knockout of
Language	English
Publishing date	2024-03-14
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.11.10.566524
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Article ; Online: Angiomotin isoform 2 promotes binding of PALS1 to KIF13B at primary cilia and regulates ciliary length and signaling.

Morthorst, Stine Kjær / Nielsen, Camilla / Farinelli, Pietro / Anvarian, Zeinab / Rasmussen, Christina Birgitte R / Serra-Marques, Andrea / Grigoriev, Ilya / Altelaar, Maarten / Fürstenberg, Nicoline / Ludwig, Alexander / Akhmanova, Anna / Christensen, Søren Tvorup / Pedersen, Lotte Bang

Journal of cell science

2022 Volume 135, Issue 12

Abstract: The kinesin-3 motor KIF13B functions in endocytosis, vesicle transport and regulation of ciliary length and signaling. Direct binding of the membrane-associated guanylate kinase (MAGUK) DLG1 to the MAGUK-binding stalk domain of KIF13B relieves motor ... ...

Abstract	The kinesin-3 motor KIF13B functions in endocytosis, vesicle transport and regulation of ciliary length and signaling. Direct binding of the membrane-associated guanylate kinase (MAGUK) DLG1 to the MAGUK-binding stalk domain of KIF13B relieves motor autoinhibition and promotes microtubule plus-end-directed cargo transport. Here, we characterize angiomotin (AMOT) isoform 2 (p80, referred to as Ap80) as a novel KIF13B interactor that promotes binding of another MAGUK, the polarity protein and Crumbs complex component PALS1, to KIF13B. Live-cell imaging analysis indicated that Ap80 is concentrated at and recruits PALS1 to the base of the primary cilium, but is not a cargo of KIF13B itself. Consistent with a ciliary function for Ap80, its depletion led to elongated primary cilia and reduced agonist-induced ciliary accumulation of SMO, a key component of the Hedgehog signaling pathway, whereas Ap80 overexpression caused ciliary shortening. Our results suggest that Ap80 activates KIF13B cargo binding at the base of the primary cilium to regulate ciliary length, composition and signaling.
MeSH term(s)	Angiomotins ; Cilia/metabolism ; Guanylate Kinases ; Hedgehog Proteins/metabolism ; Membrane Proteins/metabolism ; Protein Isoforms
Chemical Substances	Angiomotins ; Hedgehog Proteins ; Membrane Proteins ; Protein Isoforms ; Guanylate Kinases (EC 2.7.4.8)
Language	English
Publishing date	2022-06-24
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.259471
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Article ; Online: Maternal Wnt/STOP signaling promotes cell division during early Xenopus embryogenesis.

Huang, Ya-Lin / Anvarian, Zeinab / Döderlein, Gabriele / Acebron, Sergio P / Niehrs, Christof

Proceedings of the National Academy of Sciences of the United States of America

2015 Volume 112, Issue 18, Page(s) 5732–5737

Abstract: During Xenopus development, Wnt signaling is thought to function first after midblastula transition to regulate axial patterning via β-catenin-mediated transcription. Here, we report that Wnt/glycogen synthase kinase 3 (GSK3) signaling functions ... ...

Abstract	During Xenopus development, Wnt signaling is thought to function first after midblastula transition to regulate axial patterning via β-catenin-mediated transcription. Here, we report that Wnt/glycogen synthase kinase 3 (GSK3) signaling functions posttranscriptionally already in mature oocytes via Wnt/stabilization of proteins (STOP) signaling. Wnt signaling is induced in oocytes after their entry into meiotic metaphase II and declines again upon exit into interphase. Wnt signaling inhibits Gsk3 and thereby protects proteins from polyubiquitination and degradation in mature oocytes. In a protein array screen, we identify a cluster of mitotic effector proteins that are polyubiquitinated in a Gsk3-dependent manner in Xenopus. Consequently inhibition of maternal Wnt/STOP signaling, but not β-catenin signaling, leads to early cleavage arrest after fertilization. The results support a novel role for Wnt signaling in cell cycle progression independent of β-catenin.
MeSH term(s)	Animals ; Cell Cycle ; Fertilization ; Gene Expression Regulation, Developmental ; Glycogen Synthase Kinase 3/metabolism ; Glycogen Synthase Kinase 3 beta ; Humans ; Mitosis ; Oocytes/cytology ; Protein Array Analysis ; Signal Transduction ; Transcription, Genetic ; Wnt1 Protein/metabolism ; Xenopus Proteins/metabolism ; Xenopus laevis/embryology
Chemical Substances	Wnt1 Protein ; Xenopus Proteins ; Glycogen Synthase Kinase 3 beta (EC 2.7.11.1) ; GSK3B protein, Xenopus (EC 2.7.11.26) ; Glycogen Synthase Kinase 3 (EC 2.7.11.26)
Language	English
Publishing date	2015-04-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1423533112
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Article ; Online: Messing up disorder: how do missense mutations in the tumor suppressor protein APC lead to cancer?

Minde, David P / Anvarian, Zeinab / Rüdiger, Stefan Gd / Maurice, Madelon M

Molecular cancer

2011 Volume 10, Page(s) 101

Abstract: Mutations in the adenomatous polyposis coli (APC) tumor suppressor gene strongly predispose to development of gastro-intestinal tumors. Central to the tumorigenic events in APC mutant cells is the uncontrolled stabilization and transcriptional activation ...

Abstract	Mutations in the adenomatous polyposis coli (APC) tumor suppressor gene strongly predispose to development of gastro-intestinal tumors. Central to the tumorigenic events in APC mutant cells is the uncontrolled stabilization and transcriptional activation of the protein β-catenin. Many questions remain as to how APC controls β-catenin degradation. Remarkably, the large C-terminal region of APC, which spans over 2000 amino acids and includes critical regions in downregulating β-catenin, is predicted to be natively unfolded. Here we discuss how this uncommonly large disordered region may help to coordinate the multiple cellular functions of APC. Recently, a significant number of germline and somatic missense mutations in the central region of APC were linked to tumorigenesis in the colon as well as extra-intestinal tissues. We classify and localize all currently known missense mutations in the APC structure. The molecular basis by which these mutations interfere with the function of APC remains unresolved. We propose several mechanisms by which cancer-related missense mutations in the large disordered domain of APC may interfere with tumor suppressor activity. Insight in the underlying molecular events will be invaluable in the development of novel strategies to counter dysregulated Wnt signaling by APC mutations in cancer.
MeSH term(s)	Adenomatous Polyposis Coli/genetics ; Adenomatous Polyposis Coli/metabolism ; Adenomatous Polyposis Coli Protein/chemistry ; Adenomatous Polyposis Coli Protein/genetics ; Adenomatous Polyposis Coli Protein/physiology ; Animals ; Cell Transformation, Neoplastic/genetics ; Cell Transformation, Neoplastic/pathology ; Genes, APC/physiology ; Genes, Tumor Suppressor ; Humans ; Models, Biological ; Mutation, Missense/physiology ; Neoplasms/genetics ; Protein Folding ; Protein Structure, Tertiary/physiology
Chemical Substances	Adenomatous Polyposis Coli Protein
Language	English
Publishing date	2011-08-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	1476-4598
ISSN (online)	1476-4598
DOI	10.1186/1476-4598-10-101
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Article ; Online: Messing up disorder

Rüdiger Stefan GD / Anvarian Zeinab / Minde David P / Maurice Madelon M

Molecular Cancer, Vol 10, Iss 1, p

how do missense mutations in the tumor suppressor protein APC lead to cancer?

2011 Volume 101

Abstract: Summary Mutations in the adenomatous polyposis coli ( APC ) tumor suppressor gene strongly predispose to development of gastro-intestinal tumors. Central to the tumorigenic events in APC mutant cells is the uncontrolled stabilization and transcriptional ... ...

Abstract	Summary Mutations in the adenomatous polyposis coli ( APC ) tumor suppressor gene strongly predispose to development of gastro-intestinal tumors. Central to the tumorigenic events in APC mutant cells is the uncontrolled stabilization and transcriptional activation of the protein β-catenin. Many questions remain as to how APC controls β-catenin degradation. Remarkably, the large C-terminal region of APC, which spans over 2000 amino acids and includes critical regions in downregulating β-catenin, is predicted to be natively unfolded. Here we discuss how this uncommonly large disordered region may help to coordinate the multiple cellular functions of APC. Recently, a significant number of germline and somatic missense mutations in the central region of APC were linked to tumorigenesis in the colon as well as extra-intestinal tissues. We classify and localize all currently known missense mutations in the APC structure. The molecular basis by which these mutations interfere with the function of APC remains unresolved. We propose several mechanisms by which cancer-related missense mutations in the large disordered domain of APC may interfere with tumor suppressor activity. Insight in the underlying molecular events will be invaluable in the development of novel strategies to counter dysregulated Wnt signaling by APC mutations in cancer.
Keywords	Neoplasms. Tumors. Oncology. Including cancer and carcinogens ; RC254-282 ; Internal medicine ; RC31-1245 ; Medicine ; R ; DOAJ:Oncology ; DOAJ:Medicine (General) ; DOAJ:Health Sciences
Subject code	572
Language	English
Publishing date	2011-08-01T00:00:00Z
Publisher	BioMed Central
Document type	Article ; Online
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Article ; Online: Axin cancer mutants form nanoaggregates to rewire the Wnt signaling network.

Anvarian, Zeinab / Nojima, Hisashi / van Kappel, Eline C / Madl, Tobias / Spit, Maureen / Viertler, Martin / Jordens, Ingrid / Low, Teck Y / van Scherpenzeel, Revina C / Kuper, Ineke / Richter, Klaus / Heck, Albert J R / Boelens, Rolf / Vincent, Jean-Paul / Rüdiger, Stefan G D / Maurice, Madelon M

Nature structural & molecular biology

2016 Volume 23, Issue 4, Page(s) 324–332

Abstract: Signaling cascades depend on scaffold proteins that regulate the assembly of multiprotein complexes. Missense mutations in scaffold proteins are frequent in human cancer, but their relevance and mode of action are poorly understood. Here we show that ... ...

Abstract	Signaling cascades depend on scaffold proteins that regulate the assembly of multiprotein complexes. Missense mutations in scaffold proteins are frequent in human cancer, but their relevance and mode of action are poorly understood. Here we show that cancer point mutations in the scaffold protein Axin derail Wnt signaling and promote tumor growth in vivo through a gain-of-function mechanism. The effect is conserved for both the human and Drosophila proteins. Mutated Axin forms nonamyloid nanometer-scale aggregates decorated with disordered tentacles, which 'rewire' the Axin interactome. Importantly, the tumor-suppressor activity of both the human and Drosophila Axin cancer mutants is rescued by preventing aggregation of a single nonconserved segment. Our findings establish a new paradigm for misregulation of signaling in cancer and show that targeting aggregation-prone stretches in mutated scaffolds holds attractive potential for cancer treatment.
MeSH term(s)	Amino Acid Sequence ; Animals ; Axin Protein/analysis ; Axin Protein/genetics ; Axin Protein/metabolism ; Axin Protein/ultrastructure ; Cell Line ; Drosophila/chemistry ; Drosophila/genetics ; Drosophila/metabolism ; Drosophila/ultrastructure ; Drosophila Proteins/analysis ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; HEK293 Cells ; Humans ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutation, Missense ; Neoplasms/genetics ; Neoplasms/metabolism ; Neoplasms/pathology ; Point Mutation ; Protein Aggregates ; Protein Conformation ; Protein Interaction Maps ; Scattering, Small Angle ; Sequence Alignment ; Wnt Signaling Pathway ; X-Ray Diffraction
Chemical Substances	Axin Protein ; Drosophila Proteins ; Protein Aggregates
Language	English
Publishing date	2016-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2126708-X
ISSN	1545-9985 ; 1545-9993
ISSN (online)	1545-9985
ISSN	1545-9993
DOI	10.1038/nsmb.3191
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