Related Experiment Video

Updated: May 31, 2026

Quantitative Immunofluorescence Assay to Measure the Variation in Protein Levels at Centrosomes
09:39

Quantitative Immunofluorescence Assay to Measure the Variation in Protein Levels at Centrosomes

Published on: December 20, 2014

Parvulin 17 promotes microtubule assembly by its peptidyl-prolyl cis/trans isomerase activity

Alexandra Thiele1, Karolin Krentzlin, Frank Erdmann

  • 1Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany.

Journal of Molecular Biology
|July 16, 2011
PubMed

Insights

Parvulin 17, a peptidyl-prolyl cis/trans isomerase, promotes microtubule assembly by interacting with tubulin in a GTP-dependent manner. Its catalytic activity is essential for this function, impacting microtubule dynamics.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Parvulin-type peptidyl-prolyl cis/trans isomerases (PPIases) are implicated in tumor progression and Alzheimer's disease.
  • Previous research highlights the significance of PPIases in various cellular processes.

Purpose of the Study:

  • To investigate the role of parvulin 17 in microtubule assembly.
  • To elucidate the mechanism by which parvulin 17 influences microtubule formation and dynamics.

Main Methods:

  • Co-precipitation and sedimentation assays to study parvulin 17-tubulin interaction.
  • Transmission electron microscopy and microtubule polymerization assays to visualize microtubule formation.
  • Peptide microarrays to identify tubulin interaction sites on parvulin 17.
  • Confocal laser scanning microscopy to assess parvulin 17 localization and microtubule dynamics.

Main Results:

  • Parvulin 17 directly interacts with tubulin in a GTP-dependent manner, promoting microtubule assembly.
  • The peptidyl-prolyl cis/trans isomerase (PPIase) activity of parvulin 17 is crucial for its microtubule-promoting function.
  • Catalytically deficient variants and inhibitors of parvulin 17 block tubulin polymerization.
  • Tubulin binds to the substrate-binding pocket of parvulin 17, specifically interacting with an Arg-Pro-Asp motif on β-tubulin.
  • Parvulin 17 colocalizes with microtubules in the cytosol, suggesting a role in microtubule dynamics.

Conclusions:

  • Parvulin 17 is a novel regulator of microtubule assembly, functioning as a microtubule-associated protein.
  • Its PPIase activity is essential for promoting tubulin polymerization and influencing microtubule dynamics.
  • Parvulin 17's interaction with tubulin provides a molecular basis for its role in cytoskeletal organization.

More Related Videos

Combining Mitotic Cell Synchronization and High Resolution Confocal Microscopy to Study the Role of Multifunctional Cell Cycle Proteins During Mitosis08:33

Combining Mitotic Cell Synchronization and High Resolution Confocal Microscopy to Study the Role of Multifunctional Cell Cycle Proteins During Mitosis

Published on: December 5, 2017

Cell Death Associated with Abnormal Mitosis Observed by Confocal Imaging in Live Cancer Cells15:53

Cell Death Associated with Abnormal Mitosis Observed by Confocal Imaging in Live Cancer Cells

Published on: August 21, 2013

Related Concept Videos

Drugs that Stabilize Microtubules01:15

Drugs that Stabilize Microtubules

Microtubules are dynamic structures that undergo cycles of catastrophe and rescue. The microtubules play a central role in cell division by forming the spindle apparatus for segregating the chromosomes. This makes them ideal targets for regulating dividing cells in tumors and malignant cancer cells. Microtubule stabilizing drugs help stabilize the microtubule formation and promote its polymerization. Paclitaxel was the first microtubule stabilizing agent used as anticancer drug in chemotherapy...
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...
Microtubule Formation01:23

Microtubule Formation

Microtubules are dynamic structures that undergo continuous assembly and disassembly. They originate from specialized multi-protein complexes known as microtubule organizing centers or MTOCs. Within the MTOC, the point of origin of the microtubule is known as the minus end, while the end radiating outward is the plus end. Microtubules serve two primary functions — the organization of spindle complexes to separate sister chromatids during mitotic or meiotic cell division and the formation of...
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...
Destabilization of Microtubules01:45

Destabilization of Microtubules

The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
Drugs that Destabilize Microtubules01:10

Drugs that Destabilize Microtubules

Microtubules are dynamic structures and can be regulated by microtubule targeting agents (MTAs). Microtubule destabilizing drugs are a class of MTAs that destabilize and prevent microtubules' polymerization. Both natural and synthetic chemicals can be found under this class of drugs. Vincristine and vinblastine, two vinca alkaloids, and colchicine were among the first to be discovered. These drugs can affect cells in various ways, either by inducing a change in cell morphology, preventing...