Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

2.3K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.3K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

18.9K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
18.9K
The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

3.9K
The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate...
3.9K
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

2.9K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
2.9K
Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

3.0K
Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
3.0K
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.1K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.1K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Aer is a bidirectional redox sensor mediating negative chemotaxis to antibiotic-induced ROS in <i>Escherichia coli</i>.

mBio·2026
Same author

Phage Mu enlists the β-sliding clamp for late gene transcription.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Texas 2-step: a new model for YcgR::c-di-GMP action at the flagellar motor.

Journal of bacteriology·2025
Same author

Texas 2-Step: A new Model for YcgR::c-di-GMP Action at the Flagellar Motor.

bioRxiv : the preprint server for biology·2025
Same author

c-di-GMP is required for swarming in <i>E. coli</i>, producing colanic acid that acts as surfactant.

mBio·2025
Same author

Membrane-associated σ factors disrupt rRNA operon clustering in Escherichia coli.

PLoS biology·2025

Related Experiment Video

Updated: Jun 18, 2025

Biophysical Characterization of Flagellar Motor Functions
06:08

Biophysical Characterization of Flagellar Motor Functions

Published on: January 18, 2017

8.2K

Flagellar protein FliL: A many-splendored thing.

Jonathan D Partridge1, Rasika M Harshey1

  • 1Department of Molecular Biosciences and the LaMontagne Center for Infectious Diseases, The University of Texas at Austin, Austin, Texas, USA.

Molecular Microbiology
|August 3, 2024
PubMed
Summary

FliL, a bacterial flagellar protein, regulates ion flow and performs diverse functions. This review explores its location and multifaceted roles in bacterial motility and gene regulation.

Keywords:
FliLflagellamotor torquerotor biasstatorssurface sensingswarmingswimming

More Related Videos

Investigating Flagella-Driven Motility in Escherichia coli by Applying Three Established Techniques in a Series
07:59

Investigating Flagella-Driven Motility in Escherichia coli by Applying Three Established Techniques in a Series

Published on: May 10, 2020

7.6K
Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
08:02

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Published on: May 5, 2022

2.6K

Related Experiment Videos

Last Updated: Jun 18, 2025

Biophysical Characterization of Flagellar Motor Functions
06:08

Biophysical Characterization of Flagellar Motor Functions

Published on: January 18, 2017

8.2K
Investigating Flagella-Driven Motility in Escherichia coli by Applying Three Established Techniques in a Series
07:59

Investigating Flagella-Driven Motility in Escherichia coli by Applying Three Established Techniques in a Series

Published on: May 10, 2020

7.6K
Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
08:02

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Published on: May 5, 2022

2.6K

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biophysics

Background:

  • FliL is a bacterial flagellar protein.
  • It is known to associate with and regulate ion flow through the stator complex.
  • FliL has been implicated in other functions like stabilizing the flagellar rod and modulating rotor bias.

Purpose of the Study:

  • To review the diverse functions of the bacterial flagellar protein FliL.
  • To investigate the importance of FliL's location in understanding its multiple roles.
  • To resolve conflicting findings and propose new insights into FliL's mechanisms.

Main Methods:

  • Literature review of existing studies on FliL.
  • Analysis of experimental evidence regarding FliL's interactions and functions.
  • Comparative analysis across different bacterial species.

Main Results:

  • FliL's association with the stator complex is conserved across many bacterial species.
  • Evidence suggests FliL plays roles beyond ion channel regulation, including structural and regulatory functions.
  • The precise localization of FliL is critical for its diverse functional outputs.

Conclusions:

  • FliL is a multifunctional protein central to bacterial flagellar operation.
  • Understanding FliL's localization is key to deciphering its complex roles in motility and beyond.
  • Further research is needed to fully elucidate FliL's mechanisms and resolve existing discrepancies.