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Article ; Online: The cell adhesion molecule Fasciclin2 regulates brush border length and organization in Drosophila renal tubules.

Halberg, Kenneth A / Rainey, Stephanie M / Veland, Iben R / Neuert, Helen / Dornan, Anthony J / Klämbt, Christian / Davies, Shireen-Anne / Dow, Julian A T

Nature communications

2016 Volume 7, Page(s) 11266

Abstract: Multicellular organisms rely on cell adhesion molecules to coordinate cell-cell interactions, and to provide navigational cues during tissue formation. In Drosophila, Fasciclin 2 (Fas2) has been intensively studied due to its role in nervous system ... ...

Abstract	Multicellular organisms rely on cell adhesion molecules to coordinate cell-cell interactions, and to provide navigational cues during tissue formation. In Drosophila, Fasciclin 2 (Fas2) has been intensively studied due to its role in nervous system development and maintenance; yet, Fas2 is most abundantly expressed in the adult renal (Malpighian) tubule rather than in neuronal tissues. The role Fas2 serves in this epithelium is unknown. Here we show that Fas2 is essential to brush border maintenance in renal tubules of Drosophila. Fas2 is dynamically expressed during tubule morphogenesis, localizing to the brush border whenever the tissue is transport competent. Genetic manipulations of Fas2 expression levels impact on both microvilli length and organization, which in turn dramatically affect stimulated rates of fluid secretion by the tissue. Consequently, we demonstrate a radically different role for this well-known cell adhesion molecule, and propose that Fas2-mediated intermicrovillar homophilic adhesion complexes help stabilize the brush border.
MeSH term(s)	Animals ; Biological Transport ; Cell Adhesion Molecules, Neuronal/genetics ; Cell Adhesion Molecules, Neuronal/metabolism ; Drosophila melanogaster/embryology ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Gene Expression Profiling ; Gene Expression Regulation, Developmental ; Kidney Tubules/embryology ; Kidney Tubules/metabolism ; Microtubules/metabolism ; Microvilli/metabolism
Chemical Substances	Cell Adhesion Molecules, Neuronal ; fasciclin II
Language	English
Publishing date	2016-04-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2041-1723
ISSN (online)	2041-1723
DOI	10.1038/ncomms11266
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Article ; Online: Analysis of primary cilia in directional cell migration in fibroblasts.

Christensen, Søren T / Veland, Iben R / Schwab, Albrecht / Cammer, Michael / Satir, Peter

Methods in enzymology

2013 Volume 525, Page(s) 45–58

Abstract: Early studies of migrating fibroblasts showed that primary cilia orient in front of the nucleus and point toward the leading edge. Recent work has shown that primary cilia coordinate a series of signaling pathways critical to fibroblast cell migration ... ...

Abstract	Early studies of migrating fibroblasts showed that primary cilia orient in front of the nucleus and point toward the leading edge. Recent work has shown that primary cilia coordinate a series of signaling pathways critical to fibroblast cell migration during development and in wound healing. In particular, platelet-derived growth factor receptor alpha (PDGFRα) is compartmentalized to the primary cilium to activate signaling pathways that regulate reorganization of the cytoskeleton required for lamellipodium formation and directional migration in the presence of a specific ligand gradient. We summarize selected methods in analyzing ciliary function in directional cell migration, including immunofluorescence microscopy, scratch assay, and chemotaxis assay by micropipette addition of PDGFRα ligands to cultures of fibroblasts. These methods should be useful not only in studying cell migration but also more generally in delineating response pathways in cells with primary cilia.
MeSH term(s)	Animals ; Cell Line ; Cell Movement/physiology ; Cilia/metabolism ; Cilia/physiology ; Fibroblasts/cytology ; Fibroblasts/metabolism ; Mice ; Microscopy, Fluorescence ; NIH 3T3 Cells ; Signal Transduction/physiology
Language	English
Publishing date	2013
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1557-7988 ; 0076-6879
ISSN (online)	1557-7988
ISSN	0076-6879
DOI	10.1016/B978-0-12-397944-5.00003-1
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Article ; Online: KIF13B establishes a CAV1-enriched microdomain at the ciliary transition zone to promote Sonic hedgehog signalling.

Schou, Kenneth B / Mogensen, Johanne B / Morthorst, Stine K / Nielsen, Brian S / Aleliunaite, Aiste / Serra-Marques, Andrea / Fürstenberg, Nicoline / Saunier, Sophie / Bizet, Albane A / Veland, Iben R / Akhmanova, Anna / Christensen, Søren T / Pedersen, Lotte B

Nature communications

2017 Volume 8, Page(s) 14177

Abstract: Ciliary membrane composition is controlled by transition zone (TZ) proteins such as RPGRIP1, RPGRIPL and NPHP4, which are vital for balanced coordination of diverse signalling systems like the Sonic hedgehog (Shh) pathway. Activation of this pathway ... ...

Abstract	Ciliary membrane composition is controlled by transition zone (TZ) proteins such as RPGRIP1, RPGRIPL and NPHP4, which are vital for balanced coordination of diverse signalling systems like the Sonic hedgehog (Shh) pathway. Activation of this pathway involves Shh-induced ciliary accumulation of Smoothened (SMO), which is disrupted by disease-causing mutations in TZ components. Here we identify kinesin-3 motor protein KIF13B as a novel member of the RPGRIP1N-C2 domain-containing protein family and show that KIF13B regulates TZ membrane composition and ciliary SMO accumulation. KIF13B is upregulated during ciliogenesis and is recruited to the ciliary base by NPHP4, which binds to two distinct sites in the KIF13B tail region, including an RPGRIP1N-C2 domain. KIF13B and NPHP4 are both essential for establishment of a CAV1 membrane microdomain at the TZ, which in turn is required for Shh-induced ciliary SMO accumulation. Thus KIF13B is a novel regulator of ciliary TZ configuration, membrane composition and Shh signalling.
MeSH term(s)	Animals ; Caveolin 1/metabolism ; Cell Line ; Cell Membrane/metabolism ; Cell Membrane/physiology ; Cilia/physiology ; Computational Biology ; Gene Expression Profiling ; Gene Expression Regulation/physiology ; Gene Knockout Techniques ; HEK293 Cells ; Hedgehog Proteins/metabolism ; Humans ; Kinesin/genetics ; Kinesin/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; NIH 3T3 Cells ; Protein Domains/physiology ; Proteins/metabolism ; Signal Transduction/physiology ; Smoothened Receptor/metabolism ; Up-Regulation ; Zinc Finger Protein GLI1/genetics ; Zinc Finger Protein GLI1/metabolism
Chemical Substances	CAV1 protein, human ; Caveolin 1 ; GLI1 protein, human ; Hedgehog Proteins ; Membrane Proteins ; NPHP4 protein, human ; NPHP4 protein, mouse ; Proteins ; SHH protein, human ; SMO protein, human ; Smoothened Receptor ; Zinc Finger Protein GLI1 ; KIF13B protein, human (EC 3.6.1.-) ; KIF13b protein, mouse (EC 3.6.1.-) ; Kinesin (EC 3.6.4.4)
Language	English
Publishing date	2017-01-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2041-1723
ISSN (online)	2041-1723
DOI	10.1038/ncomms14177
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Article ; Online: The cell adhesion molecule Fasciclin2 regulates brush border length and organization in Drosophila renal tubules

Kenneth A. Halberg / Stephanie M. Rainey / Iben R. Veland / Helen Neuert / Anthony J. Dornan / Christian Klämbt / Shireen-Anne Davies / Julian A. T. Dow

Nature Communications, Vol 7, Iss 1, Pp 1-

2016 Volume 10

Abstract: In Drosophila, Fasciclin 2 (Fas2) has been mainly studied in the nervous system, yet this adhesion protein is more abundant in the adult renal tubule. Here the authors show that Fas2 is essential for brush border maintenance in renal tubules through ... ...

Abstract	In Drosophila, Fasciclin 2 (Fas2) has been mainly studied in the nervous system, yet this adhesion protein is more abundant in the adult renal tubule. Here the authors show that Fas2 is essential for brush border maintenance in renal tubules through regulation of microvilli length and organization.
Keywords	Science ; Q
Language	English
Publishing date	2016-04-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
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Article: Assembly of primary cilia.

Pedersen, Lotte B / Veland, Iben R / Schrøder, Jacob M / Christensen, Søren T

Developmental dynamics : an official publication of the American Association of Anatomists

2008 Volume 237, Issue 8, Page(s) 1993–2006

Abstract: Primary cilia are microtubule-based, hair-like sensory organelles present on the surface of most growth-arrested cells in our body. Recent research has demonstrated a crucial role for primary cilia in regulating vertebrate developmental pathways and ... ...

Abstract	Primary cilia are microtubule-based, hair-like sensory organelles present on the surface of most growth-arrested cells in our body. Recent research has demonstrated a crucial role for primary cilia in regulating vertebrate developmental pathways and tissue homeostasis, and defects in genes involved in primary cilia assembly or function have been associated with a panoply of disorders and diseases, including polycystic kidney disease, left-right asymmetry defects, hydrocephalus, and Bardet Biedl Syndrome. Here we provide an up-to-date review focused on the molecular mechanisms involved in the assembly of primary cilia in vertebrate cells. We present an overview of the early stages of the cilia assembly process, as well as a description of the intraflagellar transport (IFT) system. IFT is a highly conserved process required for assembly of almost all eukaryotic cilia and flagella, and much of our current knowledge about IFT is based on studies performed in Chlamydomonas and Caenorhabditis elegans. Therefore, our review of the IFT literature includes studies performed in these two model organisms. The role of several non-IFT proteins (e.g., centrosomal proteins) in the ciliary assembly process is also discussed.
MeSH term(s)	Animals ; Caenorhabditis elegans/cytology ; Chlamydomonas/cytology ; Cilia/physiology ; Eukaryotic Cells/physiology ; Eukaryotic Cells/ultrastructure ; Models, Animal
Language	English
Publishing date	2008-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1102541-4
ISSN	1097-0177 ; 1058-8388
ISSN (online)	1097-0177
ISSN	1058-8388
DOI	10.1002/dvdy.21521
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Article ; Online: KIF13B establishes a CAV1-enriched microdomain at the ciliary transition zone to promote Sonic hedgehog signalling

Kenneth B. Schou / Johanne B. Mogensen / Stine K. Morthorst / Brian S. Nielsen / Aiste Aleliunaite / Andrea Serra-Marques / Nicoline Fürstenberg / Sophie Saunier / Albane A. Bizet / Iben R. Veland / Anna Akhmanova / Søren T. Christensen / Lotte B. Pedersen

Nature Communications, Vol 8, Iss 1, Pp 1-

2017 Volume 15

Abstract: The ciliary transition zone (TZ) regulates the protein and membrane composition of the primary cilium. Here the authors identify the kinesin-3 motor protein KIF13B as a regulator of TZ membrane composition that controls the ciliary accumulation of ... ...

Abstract	The ciliary transition zone (TZ) regulates the protein and membrane composition of the primary cilium. Here the authors identify the kinesin-3 motor protein KIF13B as a regulator of TZ membrane composition that controls the ciliary accumulation of Smoothened, which is involved in activation of Sonic hedgehog signalling.
Keywords	Science ; Q
Language	English
Publishing date	2017-01-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
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Article ; Online: Primary cilia and signaling pathways in mammalian development, health and disease.

Veland, Iben R / Awan, Aashir / Pedersen, Lotte B / Yoder, Bradley K / Christensen, Søren T

Nephron. Physiology

2009 Volume 111, Issue 3, Page(s) p39–53

Abstract: Although first described as early as 1898 and long considered a vestigial organelle of little functional importance, the primary cilium has become one of the hottest research topics in modern cell biology and physiology. Primary cilia are nonmotile ... ...

Abstract	Although first described as early as 1898 and long considered a vestigial organelle of little functional importance, the primary cilium has become one of the hottest research topics in modern cell biology and physiology. Primary cilia are nonmotile sensory organelles present in a single copy on the surface of most growth-arrested or differentiated mammalian cells, and defects in their assembly or function are tightly coupled to many developmental defects, diseases and disorders. In normal tissues, the primary cilium coordinates a series of signal transduction pathways, including Hedgehog, Wnt, PDGFRalpha and integrin signaling. In the kidney, the primary cilium may function as a mechano-, chemo- and osmosensing unit that probes the extracellular environment and transmits signals to the cell via, e.g., polycystins, which depend on ciliary localization for appropriate function. Indeed, hypomorphic mutations in the mouse ift88 (previously called Tg737) gene, which encodes a ciliogenic intraflagellar transport protein, result in malformation of primary cilia, and in the collecting ducts of kidney tubules this is accompanied by development of autosomal recessive polycystic kidney disease (PKD). While PKD was one of the first diseases to be linked to dysfunctional primary cilia, defects in this organelle have subsequently been associated with many other phenotypes, including cancer, obesity, diabetes as well as a number of developmental defects. Collectively, these disorders of the cilium are now referred to as the ciliopathies. In this review, we provide a brief overview of the structure and function of primary cilia and some of their roles in coordinating signal transduction pathways in mammalian development, health and disease.
MeSH term(s)	Animals ; Cilia/metabolism ; Cilia/pathology ; Embryonic Development ; Humans ; Intracellular Signaling Peptides and Proteins/metabolism ; Kidney/metabolism ; Kidney/pathology ; Mutation ; Polycystic Kidney Diseases/metabolism ; Polycystic Kidney Diseases/pathology ; Signal Transduction ; Stem Cells/metabolism ; Stem Cells/pathology ; Tumor Suppressor Proteins/genetics ; Tumor Suppressor Proteins/metabolism
Chemical Substances	Intracellular Signaling Peptides and Proteins ; Tg737Rpw protein, mouse ; Tumor Suppressor Proteins
Language	English
Publishing date	2009-03-10
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	207121-6
ISSN	1660-2137 ; 1423-0186 ; 2235-3186 ; 1660-8151 ; 0028-2766
ISSN (online)	1660-2137 ; 1423-0186 ; 2235-3186
ISSN	1660-8151 ; 0028-2766
DOI	10.1159/000208212
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Article: The primary cilium coordinates signaling pathways in cell cycle control and migration during development and tissue repair.

Christensen, Søren T / Pedersen, Stine F / Satir, Peter / Veland, Iben R / Schneider, Linda

Current topics in developmental biology

2008 Volume 85, Page(s) 261–301

Abstract: Cell cycle control and migration are critical processes during development and maintenance of tissue functions. Recently, primary cilia were shown to take part in coordination of the signaling pathways that control these cellular processes in human ... ...

Abstract	Cell cycle control and migration are critical processes during development and maintenance of tissue functions. Recently, primary cilia were shown to take part in coordination of the signaling pathways that control these cellular processes in human health and disease. In this review, we present an overview of the function of primary cilia and the centrosome in the signaling pathways that regulate cell cycle control and migration with focus on ciliary signaling via platelet-derived growth factor receptor alpha (PDGFRalpha). We also consider how the primary cilium and the centrosome interact with the extracellular matrix, coordinate Wnt signaling, and modulate cytoskeletal changes that impinge on both cell cycle control and cell migration.
MeSH term(s)	Animals ; Cell Cycle/physiology ; Cell Movement ; Cilia/physiology ; Receptor, Platelet-Derived Growth Factor alpha/metabolism ; Regeneration ; Signal Transduction/physiology ; Tissue Engineering
Chemical Substances	Receptor, Platelet-Derived Growth Factor alpha (EC 2.7.10.1)
Language	English
Publishing date	2008
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ISSN	1557-8933 ; 0070-2153
ISSN (online)	1557-8933
ISSN	0070-2153
DOI	10.1016/S0070-2153(08)00810-7
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Article ; Online: Inversin/Nephrocystin-2 is required for fibroblast polarity and directional cell migration.

Veland, Iben R / Montjean, Rodrick / Eley, Lorraine / Pedersen, Lotte B / Schwab, Albrecht / Goodship, Judith / Kristiansen, Karsten / Pedersen, Stine F / Saunier, Sophie / Christensen, Søren T

PloS one

2013 Volume 8, Issue 4, Page(s) e60193

Abstract: Inversin is a ciliary protein that critically regulates developmental processes and tissue homeostasis in vertebrates, partly through the degradation of Dishevelled (Dvl) proteins to coordinate Wnt signaling in planar cell polarity (PCP). Here, we ... ...

Abstract	Inversin is a ciliary protein that critically regulates developmental processes and tissue homeostasis in vertebrates, partly through the degradation of Dishevelled (Dvl) proteins to coordinate Wnt signaling in planar cell polarity (PCP). Here, we investigated the role of Inversin in coordinating cell migration, which highly depends on polarity processes at the single-cell level, including the spatial and temporal organization of the cytoskeleton as well as expression and cellular localization of proteins in leading edge formation of migrating cells. Using cultures of mouse embryonic fibroblasts (MEFs) derived from inv(-/-) and inv(+/+) animals, we confirmed that both inv(-/-) and inv(+/+) MEFs form primary cilia, and that Inversin localizes to the primary cilium in inv(+/+) MEFs. In wound healing assays, inv(-/-) MEFs were severely compromised in their migratory ability and exhibited cytoskeletal rearrangements, including distorted lamellipodia formation and cilia orientation. Transcriptome analysis revealed dysregulation of Wnt signaling and of pathways regulating actin organization and focal adhesions in inv(-/-) MEFs as compared to inv(+/+) MEFs. Further, Dvl-1 and Dvl-3 localized to MEF primary cilia, and β-catenin/Wnt signaling was elevated in inv(-/-) MEFs, which moreover showed reduced ciliary localization of Dvl-3. Finally, inv(-/-) MEFs displayed dramatically altered activity and localization of RhoA, Rac1, and Cdc42 GTPases, and aberrant expression and targeting of the Na(+)/H(+) exchanger NHE1 and ezrin/radixin/moesin (ERM) proteins to the edge of cells facing the wound. Phosphorylation of β-catenin at the ciliary base and formation of well-defined lamellipodia with localization and activation of ERM to the leading edge of migrating cells were restored in inv(-/-) MEFs expressing Inv-GFP. Collectively, our findings point to the significance of Inversin in controlling cell migration processes, at least in part through transcriptional regulation of genes involved in Wnt signaling and pathways that control cytoskeletal organization and ion transport.
MeSH term(s)	Animals ; Cell Line ; Cell Movement ; Cell Polarity ; Cilia/metabolism ; Cytoskeleton/metabolism ; Enzyme Activation ; Female ; Fibroblasts/cytology ; Fibroblasts/metabolism ; Gene Expression Regulation ; Mice ; Pregnancy ; Protein Transport ; Pseudopodia/metabolism ; Signal Transduction ; Transcription Factors/deficiency ; Transcription Factors/metabolism ; Transcriptome ; Wnt Proteins/metabolism ; Wound Healing ; beta Catenin/metabolism ; rho GTP-Binding Proteins/metabolism
Chemical Substances	Invs protein, mouse ; Transcription Factors ; Wnt Proteins ; beta Catenin ; rho GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2013-04-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0060193
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Article ; Online: Inversin/Nephrocystin-2 is required for fibroblast polarity and directional cell migration.

Iben R Veland / Rodrick Montjean / Lorraine Eley / Lotte B Pedersen / Albrecht Schwab / Judith Goodship / Karsten Kristiansen / Stine F Pedersen / Sophie Saunier / Søren T Christensen

PLoS ONE, Vol 8, Iss 4, p e

2013 Volume 60193

Abstract	Inversin is a ciliary protein that critically regulates developmental processes and tissue homeostasis in vertebrates, partly through the degradation of Dishevelled (Dvl) proteins to coordinate Wnt signaling in planar cell polarity (PCP). Here, we investigated the role of Inversin in coordinating cell migration, which highly depends on polarity processes at the single-cell level, including the spatial and temporal organization of the cytoskeleton as well as expression and cellular localization of proteins in leading edge formation of migrating cells. Using cultures of mouse embryonic fibroblasts (MEFs) derived from inv(-/-) and inv(+/+) animals, we confirmed that both inv(-/-) and inv(+/+) MEFs form primary cilia, and that Inversin localizes to the primary cilium in inv(+/+) MEFs. In wound healing assays, inv(-/-) MEFs were severely compromised in their migratory ability and exhibited cytoskeletal rearrangements, including distorted lamellipodia formation and cilia orientation. Transcriptome analysis revealed dysregulation of Wnt signaling and of pathways regulating actin organization and focal adhesions in inv(-/-) MEFs as compared to inv(+/+) MEFs. Further, Dvl-1 and Dvl-3 localized to MEF primary cilia, and β-catenin/Wnt signaling was elevated in inv(-/-) MEFs, which moreover showed reduced ciliary localization of Dvl-3. Finally, inv(-/-) MEFs displayed dramatically altered activity and localization of RhoA, Rac1, and Cdc42 GTPases, and aberrant expression and targeting of the Na(+)/H(+) exchanger NHE1 and ezrin/radixin/moesin (ERM) proteins to the edge of cells facing the wound. Phosphorylation of β-catenin at the ciliary base and formation of well-defined lamellipodia with localization and activation of ERM to the leading edge of migrating cells were restored in inv(-/-) MEFs expressing Inv-GFP. Collectively, our findings point to the significance of Inversin in controlling cell migration processes, at least in part through transcriptional regulation of genes involved in Wnt signaling and pathways that ...
Keywords	Medicine ; R ; Science ; Q
Subject code	571
Language	English
Publishing date	2013-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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