Dynamic rearrangement of nucleoporins during fungal "open" mitosis

Ulrike Theisen1, Anne Straube, Gero Steinberg

  • 1Max-Planck-Institut für terrestrische Mikrobiologie, D-35043 Marburg, Germany.

Insights

Nuclear pore complex proteins dynamically reorganize during open mitosis in the corn smut fungus Ustilago maydis. These findings reveal conserved principles of nuclear envelope and pore assembly in fungi.

Area of Science:

  • Cell Biology
  • Mycology
  • Molecular Biology

Background:

  • Animal mitosis involves nuclear envelope breakdown, unlike most fungi.
  • The corn smut fungus Ustilago maydis exhibits an 'open' mitosis with nuclear envelope removal.

Purpose of the Study:

  • To investigate the dynamic behavior of key nucleoporins during open mitosis in Ustilago maydis.
  • To understand the assembly and dynamics of nuclear pore complexes in a fungal model with open mitosis.

Main Methods:

  • Tracking nucleoporins (Nup214, Pom152, Nup133, Nup107) during mitosis.
  • Observing nuclear envelope and nuclear pore complex (NPC) assembly and disassembly.
  • Assessing the role of microtubules and F-actin in NPC formation.

Main Results:

  • Nuclear pore complexes disassembled in prophase; nucleoporins dispersed.
  • Nup107 and Nup133 localized to chromosomes during metaphase and anaphase.
  • Nuclear envelope reformation and NPC assembly occurred, with subsequent protein import.
  • NPC assembly was independent of microtubules or F-actin alone but disrupted if both were absent.

Conclusions:

  • The dynamic behavior of nucleoporins during open mitosis in Ustilago maydis is described.
  • Nuclear pore complex and nuclear envelope assembly principles appear conserved despite open mitosis.
  • Cytoskeletal elements play a role in nuclear envelope and pore complex formation.

Related Concept Videos

Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

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...
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
Forces Acting on Chromosomes02:11

Forces Acting on Chromosomes

During mitosis, chromosome movements occur through the interplay of multiple piconewton level forces. In prometaphase, these forces help in chromosome assembly or congression at the equatorial plane, eventually leading to their alignment at the metaphase plate. The forces acting on the chromosomes are space and time-dependent; therefore, they vary with the position of the chromosomes as the cell progresses through mitosis. 
Microtubules and motor proteins exert two types of forces on...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
Anaphase A and B01:39

Anaphase A and B

Microtubules form through the end-to-end polymerization of tubulin heterodimers. Kinetochore microtubules originate from the spindle poles, and their plus-ends connect with the kinetochores on sister-chromatids. Ndc80 protein complexes, present on the kinetochore, form low-affinity links with the plus end of these kinetochore microtubules.
Plus-end depolymerization releases tubulin heterodimers from the terminal region of the microtubule. As tubulin subunits are lost, the Ndc80 complexes detach...
Nucleosome Remodeling02:54

Nucleosome Remodeling

Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...