Skip to main content

Main menu

  • Home
  • Content
    • Published Ahead of Print
    • Current Issue
    • JASN Podcasts
    • Article Collections
    • Archives
    • Kidney Week Abstracts
    • Saved Searches
  • Authors
    • Submit a Manuscript
    • Author Resources
  • Editorial Team
  • Editorial Fellowship
    • Editorial Fellowship Team
    • Editorial Fellowship Application Process
  • More
    • About JASN
    • Advertising
    • Alerts
    • Feedback
    • Impact Factor
    • Reprints
    • Subscriptions
  • ASN Kidney News
  • Other
    • ASN Publications
    • CJASN
    • Kidney360
    • Kidney News Online
    • American Society of Nephrology

User menu

  • Subscribe
  • My alerts
  • Log in
  • My Cart

Search

  • Advanced search
American Society of Nephrology
  • Other
    • ASN Publications
    • CJASN
    • Kidney360
    • Kidney News Online
    • American Society of Nephrology
  • Subscribe
  • My alerts
  • Log in
  • My Cart
Advertisement
American Society of Nephrology

Advanced Search

  • Home
  • Content
    • Published Ahead of Print
    • Current Issue
    • JASN Podcasts
    • Article Collections
    • Archives
    • Kidney Week Abstracts
    • Saved Searches
  • Authors
    • Submit a Manuscript
    • Author Resources
  • Editorial Team
  • Editorial Fellowship
    • Editorial Fellowship Team
    • Editorial Fellowship Application Process
  • More
    • About JASN
    • Advertising
    • Alerts
    • Feedback
    • Impact Factor
    • Reprints
    • Subscriptions
  • ASN Kidney News
  • Follow JASN on Twitter
  • Visit ASN on Facebook
  • Follow JASN on RSS
  • Community Forum
Molecular Medicine, Genetics and Development
You have accessRestricted Access

The Polycystic Kidney Disease Proteins, Polycystin-1, Polycystin-2, Polaris, and Cystin, Are Co-Localized in Renal Cilia

Bradley K. Yoder, Xiaoying Hou and Lisa M. Guay-Woodford
JASN October 2002, 13 (10) 2508-2516; DOI: https://doi.org/10.1097/01.ASN.0000029587.47950.25
Bradley K. Yoder
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Xiaoying Hou
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Lisa M. Guay-Woodford
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • Article
  • Figures & Data Supps
  • Info & Metrics
  • View PDF
Loading

Abstract

ABSTRACT. Recent evidence has suggested an association between structural and/or functional defects in the primary apical cilium of vertebrate epithelia and polycystic kidney disease (PKD). In Caenorhabditis elegans, the protein orthologues of the PKD-related proteins, polycystin-1 (LOV-1), polycystin-2 (PKD2), and polaris (OSM-5), co-localize in the cilia of male-specific sensory neurons, and defects in these proteins cause abnormalities of cilia structure and/or function. This study sought to determine whether the mammalian polycystins are expressed in primary cilia of renal epithelia and whether these proteins co-localize with polaris and cystin, the newly described, cilia-associated protein that is disrupted in the cpk mouse. To begin to address this issue, the expression of the protein products encoded by the PKD1, PKD2, Tg737, and cpk genes were examined in mouse cortical collecting duct (mCCD) cells using an immunofluorescence-based approach with a series of previously well-characterized antibodies. The mCCD cells were grown on cell culture inserts to optimize cell polarization and cilia formation. The data demonstrate co-localization in cilia of polycystin-1 and polycystin-2, which are the principal proteins involved in autosomal dominant polycystic kidney disease, with polaris and cystin, which are proteins that are disrupted in the Tg737orpkand cpk mouse models of autosomal recessive polycystic kidney disease, respectively. These data add to a growing body of evidence that suggests that primary cilium plays a key role in normal physiologic functions of renal epithelia and that defects in ciliary function contribute to the pathogenesis of PKD.E-mail:lgw@uab.edu

  • © 2002 American Society of Nephrology
View Full Text
PreviousNext
Back to top

In this issue

Journal of the American Society of Nephrology: 13 (10)
Journal of the American Society of Nephrology
Vol. 13, Issue 10
1 Oct 2002
  • Table of Contents
  • Index by author
View Selected Citations (0)
Print
Download PDF
Sign up for Alerts
Email Article
Thank you for your help in sharing the high-quality science in JASN.
Enter multiple addresses on separate lines or separate them with commas.
The Polycystic Kidney Disease Proteins, Polycystin-1, Polycystin-2, Polaris, and Cystin, Are Co-Localized in Renal Cilia
(Your Name) has sent you a message from American Society of Nephrology
(Your Name) thought you would like to see the American Society of Nephrology web site.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Citation Tools
The Polycystic Kidney Disease Proteins, Polycystin-1, Polycystin-2, Polaris, and Cystin, Are Co-Localized in Renal Cilia
Bradley K. Yoder, Xiaoying Hou, Lisa M. Guay-Woodford
JASN Oct 2002, 13 (10) 2508-2516; DOI: 10.1097/01.ASN.0000029587.47950.25

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
Request Permissions
Share
The Polycystic Kidney Disease Proteins, Polycystin-1, Polycystin-2, Polaris, and Cystin, Are Co-Localized in Renal Cilia
Bradley K. Yoder, Xiaoying Hou, Lisa M. Guay-Woodford
JASN Oct 2002, 13 (10) 2508-2516; DOI: 10.1097/01.ASN.0000029587.47950.25
del.icio.us logo Digg logo Reddit logo Twitter logo Facebook logo Google logo Mendeley logo
  • Tweet Widget
  • Facebook Like

Jump to section

  • Article
    • Abstract
    • Materials and Methods
    • Results
    • Discussion
    • Acknowledgments
    • References
  • Figures & Data Supps
  • Info & Metrics
  • View PDF

More in this TOC Section

  • Glomerular and Renal Vascular Structural Changes in α8 Integrin-Deficient Mice
  • Analysis of the Polycystins in Aortic Vascular Smooth Muscle Cells
  • Autosomal Dominant Progressive Nephropathy with Deafness: Linkage to a New Locus on Chromosome 11q24
Show more Molecular Medicine, Genetics and Development

Cited By...

  • Ly6chi Infiltrating Macrophages Promote Cyst Progression in Injured Conditional Ift88 Mice
  • Pkd1 and Wnt5a genetically interact to control lymphatic vascular morphogenesis in mice
  • Organelle Stress and Crosstalk in Kidney Disease
  • GDNF drives rapid tubule morphogenesis in a novel 3D in vitro model for ADPKD
  • Loss of polycystins suppresses deciliation via the activation of the centrosomal integrity pathway
  • Disease Modeling To Understand the Pathomechanisms of Human Genetic Kidney Disorders
  • Ca2+-Dependent Regulation by the Cyclic AMP Pathway of Primary Cilium Length in LLC-PK1 Renal Epithelial Cells
  • Polycystin-2 (TRPP2) Regulates Primary Cilium Length in LLC-PK1 Renal Epithelial Cells
  • Cystin gene mutations cause autosomal recessive polycystic kidney disease associated with altered Myc expression
  • Primary cilia and the exocyst are linked to urinary extracellular vesicle production and content
  • Synergistic Genetic Interactions between Pkhd1 and Pkd1 Result in an ARPKD-Like Phenotype in Murine Models
  • Tissue-Resident Macrophages Promote Renal Cystic Disease
  • The cilium as a force sensor-myth versus reality
  • The Ciliary Lumen Accommodates Passive Diffusion and Vesicle Trafficking in Cytoplasmic-Ciliary Transport
  • Three-dimensional architecture of epithelial primary cilia
  • Polycystin 2 regulates mitochondrial Ca2+ signaling, bioenergetics, and dynamics through mitofusin 2
  • PKD2 is an essential ion channel subunit in the primary cilium of the renal collecting duct epithelium
  • Human-Specific Abnormal Alternative Splicing of Wild-Type PKD1 Induces Premature Termination of Polycystin-1
  • Retromer associates with the cytoplasmic amino-terminus of polycystin-2
  • Cell-cell communication via ciliary extracellular vesicles: clues from model systems
  • Polycystin 1 loss of function is directly linked to an imbalance in G-protein signaling in the kidney
  • Ciliary Mechanisms of Cyst Formation in Polycystic Kidney Disease
  • The ciliary membrane-associated proteome reveals actin-binding proteins as key components of cilia
  • BLOC-1 is required for selective membrane protein trafficking from endosomes to primary cilia
  • Tubby family proteins are adapters for ciliary trafficking of integral membrane proteins
  • Trafficking to the primary cilium membrane
  • Progress in ciliary ion channel physiology
  • Deletion of ADP Ribosylation Factor-Like GTPase 13B Leads to Kidney Cysts
  • Extracellular Vesicles in Renal Diseases: More than Novel Biomarkers?
  • Regulation of polycystin-1 ciliary trafficking by motifs at its C-terminus and polycystin-2 but not by cleavage at the GPS site
  • New frontiers: discovering cilia-independent functions of cilia proteins
  • The cAMP Signaling Pathway and Direct Protein Kinase A Phosphorylation Regulate Polycystin-2 (TRPP2) Channel Function
  • Chemical and Physical Sensors in the Regulation of Renal Function
  • The Future of Polycystic Kidney Disease Research--As Seen By the 12 Kaplan Awardees
  • Myristoylated CIL-7 regulates ciliary extracellular vesicle biogenesis
  • TMEM231, mutated in orofaciodigital and Meckel syndromes, organizes the ciliary transition zone
  • Inactivation of Integrin-{beta}1 Prevents the Development of Polycystic Kidney Disease after the Loss of Polycystin-1
  • TRPP2-dependent Ca2+ signaling in dorso-lateral mesoderm is required for kidney field establishment in Xenopus
  • Aberrant Glycosylation and Localization of Polycystin-1 Cause Polycystic Kidney in an AQP11 Knockout Model
  • Novel Functional Complexity of Polycystin-1 by GPS Cleavage In Vivo: Role in Polycystic Kidney Disease
  • The exocyst and regulatory GTPases in urinary exosomes
  • Rapid and Efficient Differentiation of Human Pluripotent Stem Cells into Intermediate Mesoderm That Forms Tubules Expressing Kidney Proximal Tubular Markers
  • Proximal Tubule Proliferation Is Insufficient to Induce Rapid Cyst Formation after Cilia Disruption
  • Loss of the Ciliary Kinase Nek8 Causes Left-Right Asymmetry Defects
  • c-Met and NF-{kappa}B-Dependent Overexpression of Wnt7a and -7b and Pax2 Promotes Cystogenesis in Polycystic Kidney Disease
  • Disruption of Kif3a in osteoblasts results in defective bone formation and osteopenia
  • Direct role of Bardet-Biedl syndrome proteins in transcriptional regulation
  • Epitope-Tagged Pkhd1 Tracks the Processing, Secretion, and Localization of Fibrocystin
  • A conserved signal and GTPase complex are required for the ciliary transport of polycystin-1
  • Polycystin-1 Is Required for Stereocilia Structure But Not for Mechanotransduction in Inner Ear Hair Cells
  • Loss of Primary Cilia Upregulates Renal Hypertrophic Signaling and Promotes Cystogenesis
  • Heterotrimeric kinesin-II is necessary and sufficient to promote different stepwise assembly of morphologically distinct bipartite cilia in Drosophila antenna
  • Pkd1l1 complexes with Pkd2 on motile cilia and functions to establish the left-right axis
  • Polycystin-2 takes different routes to the somatic and ciliary plasma membrane
  • The human polycystin-2 protein represents an integral membrane protein with six membrane-spanning domains and intracellular N- and C-termini
  • Prefoldin 5 Is Required for Normal Sensory and Neuronal Development in a Murine Model
  • The cell biology of polycystic kidney disease
  • The zebrafish foxj1a transcription factor regulates cilia function in response to injury and epithelial stretch
  • The Role of Transient Receptor Potential Cation Channels in Ca2+ Signaling
  • The ADPKD genes pkd1a/b and pkd2 regulate extracellular matrix formation
  • Synergistic Interaction between Ciliary Genes Reflects the Importance of Mutational Load in Ciliopathies
  • A polycystin-2 (TRPP2) dimerization domain essential for the function of heteromeric polycystin complexes
  • The primary cilium at a glance
  • Cystin Localizes to Primary Cilia via Membrane Microdomains and a Targeting Motif
  • Cystin, Cilia, and Cysts: Unraveling Trafficking Determinants
  • Type II Calcimimetics and Polycystic Kidney Disease: Unanswered Questions
  • 2008 Homer W. Smith Award: Insights into the Pathogenesis of Polycystic Kidney Disease from Gene Discovery
  • A Mouse Model for Meckel Syndrome Type 3
  • Characterization of PKD Protein-Positive Exosome-Like Vesicles
  • Targeting Cyst Initiation in ADPKD
  • Syntaxin 5 regulates the endoplasmic reticulum channel-release properties of polycystin-2
  • Role of Vasopressin Antagonists
  • Polycystic Kidneys Caused by Sustained Expression of Cux1 Isoform p75
  • Endothelial Cilia Are Fluid Shear Sensors That Regulate Calcium Signaling and Nitric Oxide Production Through Polycystin-1
  • Nek8 Regulates the Expression and Localization of Polycystin-1 and Polycystin-2
  • The cell biological basis of ciliary disease
  • Google Scholar

Similar Articles

Related Articles

  • No related articles found.
  • PubMed
  • Google Scholar

Articles

  • Current Issue
  • Early Access
  • Subject Collections
  • Article Archive
  • ASN Annual Meeting Abstracts

Information for Authors

  • Submit a Manuscript
  • Author Resources
  • Editorial Fellowship Program
  • ASN Journal Policies
  • Reuse/Reprint Policy

About

  • JASN
  • ASN
  • ASN Journals
  • ASN Kidney News

Journal Information

  • About JASN
  • JASN Email Alerts
  • JASN Key Impact Information
  • JASN Podcasts
  • JASN RSS Feeds
  • Editorial Board

More Information

  • Advertise
  • ASN Podcasts
  • ASN Publications
  • Become an ASN Member
  • Feedback
  • Follow on Twitter
  • Password/Email Address Changes
  • Subscribe to ASN Journals

© 2022 American Society of Nephrology

Print ISSN - 1046-6673 Online ISSN - 1533-3450

Powered by HighWire