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Related Concept Videos

Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
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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.
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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.
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Directionality of Nuclear Transport01:42

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Ras-related nuclear protein or Ran is a small G protein that cycles between its GTP and GDP bound states. Ran specific regulators, a Ran GTPase Activating Protein or RanGAP present in the cytosol and a Ran guanine nucleotide exchange factor or RanGEF present inside the nucleus regulate GTP/GDP exchange. A high concentration of GTP inside the cells, in addition to this asymmetric distribution of  Ran-specific regulators, leads to a higher RanGTP concentration inside the nucleus. This...
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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
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A Novel Stretching Platform for Applications in Cell and Tissue Mechanobiology
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Published on: June 3, 2014

Modulation of Nuclear Shape by Substrate Rigidity.

David B Lovett1, Nandini Shekhar, Jeffrey A Nickerson

  • 1Department of Chemical Engineering, University of Florida, Bldg. 723, Gainesville, FL 32611, USA.

Cellular and Molecular Bioengineering
|August 6, 2013
PubMed
Summary
This summary is machine-generated.

Cell nuclei change shape based on the stiffness of their environment, a process dependent on the Linker of Nucleoskeleton to Cytoskeleton (LINC) complex and actomyosin tension. This mechanical coupling influences cell behavior.

Keywords:
LINC complexMechanosensingNucleusPolyacrylamide gelsSubstrate rigidity

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Biophysical Assays to Probe the Mechanical Properties of the Interphase Cell Nucleus: Substrate Strain Application and Microneedle Manipulation
16:27

Biophysical Assays to Probe the Mechanical Properties of the Interphase Cell Nucleus: Substrate Strain Application and Microneedle Manipulation

Published on: September 14, 2011

Area of Science:

  • Cell Biology
  • Biophysics
  • Mechanobiology

Background:

  • The cell nucleus is mechanically connected to the cytoskeleton via the LINC complex.
  • Mechanical forces from the extracellular matrix can transmit to the nuclear surface through the cytoskeleton.

Purpose of the Study:

  • To quantify nuclear shape changes in response to substrate rigidity.
  • To investigate the role of the LINC complex and actomyosin tension in nuclear shape modulation and rigidity sensing.

Main Methods:

  • NIH 3T3 fibroblasts cultured on polyacrylamide gels of varying stiffness (0.4 kPa to 308 kPa).
  • Quantification of nuclear shape in vertical cross-section.
  • Manipulation of the LINC complex (dominant negative KASH domains) and actomyosin activity (myosin inhibition).
  • Assessment of cell motility and spreading.

Main Results:

  • Nuclear shape was sensitive to substrate rigidity, appearing rounded on soft substrates and flattened on stiff substrates.
  • Disruption of the LINC complex abolished nuclear shape sensitivity to substrate rigidity.
  • Myosin inhibition similarly affected nuclear shape response to substrate stiffness.
  • Over-expression of GFP-KASH4 impacted rigidity-dependent cell motility and spreading.

Conclusions:

  • Nuclear shape is modulated by actomyosin tension, which is influenced by substrate rigidity.
  • A mechanically integrated nucleus-cytoskeleton system is essential for sensing substrate rigidity.
  • Substrate rigidity may control nuclear and cellular functions through mechanical signaling pathways.