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Related Concept Videos

Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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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...
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Disassembly of Intermediate Filaments01:35

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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...
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Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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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...
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Mechanism of Filopodia Formation01:39

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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.
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Catenins01:23

Catenins

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Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
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Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
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Related Experiment Video

Updated: Sep 13, 2025

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Filamentation of hCTPS1 with CTP.

Chen-Jun Guo1, Xiaojie Bao1, Ji-Long Liu2,3

  • 1School of Life Science and Technology, ShanghaiTech University, Shanghai, China.

Cell & Bioscience
|July 30, 2025
PubMed
Summary

Cytidine triphosphate (CTP) synthase 1 (CTPS1) forms filaments regulated by its product, CTP. This cryo-EM study reveals conserved mechanisms for CTPS1 regulation, offering therapeutic targets for cancer and immune diseases.

Keywords:
CTP synthaseCryo-EMCytoophidiumMetabolic filamentProduct feedback regulation

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Cytidine triphosphate (CTP) synthase (CTPS) is crucial for nucleotide synthesis and cell proliferation.
  • Human CTPS1 (hCTPS1) is vital for immune responses and highly expressed in proliferating cells, indicating its potential as a therapeutic target.
  • Regulatory mechanisms of hCTPS1 activity are not well understood.

Purpose of the Study:

  • To investigate the regulatory mechanisms of human CTPS1 (hCTPS1) activity.
  • To elucidate the role of CTP in hCTPS1 filamentation and regulation.
  • To understand the structural basis of CTP binding and filament assembly in hCTPS1.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine the structure of CTP-bound hCTPS1 filaments.
  • Biochemical assays to analyze CTP's regulatory role.
  • Comparative analysis of CTP-binding pockets across species.

Main Results:

  • CTP acts as a key regulator of hCTPS1 filamentation.
  • High-resolution cryo-EM structures reveal molecular details of CTP binding and filament assembly.
  • CTP generated during enzymatic activity does not induce filament disassembly, indicating a conserved regulatory pattern.
  • Filamentation mechanism is evolutionarily conserved in eukaryotic CTPS.

Conclusions:

  • CTP binding regulates hCTPS1 activity through filamentation.
  • The study reveals a novel, conserved regulatory mechanism for metabolic enzymes.
  • Findings provide insights for developing targeted therapies for immune-related diseases and cancer by targeting hCTPS1.