Related Experiment Video

Updated: Jun 9, 2026

Reconstitution of Membrane-Tethered Minimal Actin Cortices on Supported Lipid Bilayers
11:55

Reconstitution of Membrane-Tethered Minimal Actin Cortices on Supported Lipid Bilayers

Published on: July 12, 2022

CEP290 tethers flagellar transition zone microtubules to the membrane and regulates flagellar protein content

Branch Craige1, Che-Chia Tsao, Dennis R Diener

  • 1Department of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA.

The Journal of Cell Biology
|September 8, 2010
PubMed

Insights

CEP290 protein is crucial for maintaining flagellar structure by anchoring the membrane to microtubules. Its absence disrupts flagellar assembly and protein composition, linking it to cilia-related disorders.

Area of Science:

  • Cell Biology
  • Genetics
  • Biochemistry

Background:

  • CEP290 mutations cause human ciliopathies, including blindness and perinatal lethality.
  • The precise function of CEP290 in cilia assembly and maintenance remains incompletely understood.

Purpose of the Study:

  • To investigate the role of CEP290 in flagellar structure and function using a Chlamydomonas reinhardtii mutant model.
  • To elucidate the localization and molecular interactions of CEP290 within the flagellum.

Main Methods:

  • Generated a Chlamydomonas reinhardtii mutant with a large deletion in the CEP290 gene.
  • Utilized immunoelectron microscopy for subcellular localization studies.
  • Performed ultrastructural and biochemical analyses of isolated flagella.
  • Investigated CEP290 dynamics using dikaryon experiments.

Main Results:

  • CEP290 localizes to the flagellar transition zone, associated with microtubule-membrane links.
  • Mutant flagella exhibit defective microtubule-membrane connectors and loss of flagellar membrane attachment.
  • Abnormal protein content, including intraflagellar transport and ciliopathy-associated proteins, was observed in mutant flagella.
  • CEP290 demonstrates dynamic behavior and rapid turnover at the transition zone.

Conclusions:

  • CEP290 is essential for forming and maintaining microtubule-membrane linkers in the flagellar transition zone.
  • CEP290 plays a critical role in regulating flagellar protein composition.
  • These findings provide insights into the molecular mechanisms underlying CEP290-related ciliopathies.

More Related Videos

Super-resolution Imaging of the Bacterial Division Machinery08:47

Super-resolution Imaging of the Bacterial Division Machinery

Published on: January 21, 2013

Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast11:19

Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast

Published on: February 20, 2017

Related Concept Videos

Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
Microtubules in Cell Motility01:24

Microtubules in Cell Motility

Microtubules are thick hollow cylindrical proteins that help form the cytoskeleton. Microtubules have varied roles in the cell. These filaments help form cellular appendages like cilia and flagella, which are responsible for locomotion. The cilia arise from basal bodies, separated from the main body by a membrane-like structure forming the transition zone. This zone is the gate for the entry of lipids and proteins, creating a unique composition of lipids and proteins in the ciliary membrane and...
Microtubules in Cell Motility01:24

Microtubules in Cell Motility

Microtubules are thick hollow cylindrical proteins that help form the cytoskeleton. Microtubules have varied roles in the cell. These filaments help form cellular appendages like cilia and flagella, which are responsible for locomotion. The cilia arise from basal bodies, separated from the main body by a membrane-like structure forming the transition zone. This zone is the gate for the entry of lipids and proteins, creating a unique composition of lipids and proteins in the ciliary membrane and...
Microtubule Associated Motor Proteins01:32

Microtubule Associated Motor Proteins

Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular cargos...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...