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Related Concept Videos

Additional Subnuclear Structures02:10

Additional Subnuclear Structures

The eukaryotic nucleus is a double membrane-bound organelle that contains nearly all of the cell’s genetic material in the form of chromosomes. It is rightly called the “brain” of the cell as it shoulders the responsibility of responding to various physiological processes, stress, altered metabolic conditions, and other cellular signals. 
The nucleus contains many membrane-less subnuclear organelles or nuclear bodies, such as nucleoli, Cajal bodies, speckles, paraspeckles, etc. These nuclear...
Additional Subnuclear Structures02:10

Additional Subnuclear Structures

The eukaryotic nucleus is a double membrane-bound organelle that contains nearly all of the cell’s genetic material in the form of chromosomes. It is rightly called the “brain” of the cell as it shoulders the responsibility of responding to various physiological processes, stress, altered metabolic conditions, and other cellular signals. 
The nucleus contains many membrane-less subnuclear organelles or nuclear bodies, such as nucleoli, Cajal bodies, speckles, paraspeckles, etc. These nuclear...
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...
Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
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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Related Experiment Video

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Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
09:02

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner

Published on: December 10, 2015

Structural insights into SUN-KASH complexes across the nuclear envelope.

Wenjia Wang1, Zhubing Shi, Shi Jiao

  • 1State Key Laboratory of Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China.

Cell Research
|September 5, 2012
PubMed
Summary
This summary is machine-generated.

The structure of the SUN2-KASH complex reveals how Linker of the nucleoskeleton and the cytoskeleton (LINC) complexes bind. This provides insights into nuclear-cytoplasmic connections and cell migration.

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Last Updated: May 19, 2026

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
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Published on: December 10, 2015

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Published on: July 29, 2018

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09:33

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Published on: October 15, 2019

Area of Science:

  • Cell biology
  • Structural biology
  • Biochemistry

Background:

  • Linker of the nucleoskeleton and the cytoskeleton (LINC) complexes connect the nucleus and cytoplasm.
  • LINC complexes are crucial for nuclear positioning, cell polarization, and cellular stiffness.
  • Previous work elucidated the homotrimeric structure of human SUN2.

Purpose of the Study:

  • To determine the crystal structure of the human SUN2-KASH complex.
  • To elucidate the molecular interactions between SUN2 and KASH proteins.
  • To understand the structural basis of LINC complex function.

Main Methods:

  • X-ray crystallography to determine the SUN2-KASH complex structure.
  • Biochemical assays to assess SUN-KASH domain interactions.
  • Cell transfection experiments to evaluate the impact of SUN2 mutations on cell migration.

Main Results:

  • The crystal structure reveals SUN2 homotrimer binding to three KASH peptides.
  • A major conformational change occurs in the AA'-loop of SUN2 upon KASH binding.
  • The PPPT motif of KASH binds to the SUN2 BI-pocket, stabilized by hydrophobic and hydrogen bonding interactions.
  • Mutations at binding sites disrupt SUN-KASH association.
  • Wild-type SUN2, but not mutants, promotes cell migration in Ovcar-3 cells.

Conclusions:

  • A structural model for the LINC complex (SUN2-KASH) has been determined.
  • The findings provide a detailed understanding of the interactions mediating the physical and functional coupling between the cytoplasm and nucleoplasm.
  • This structural insight is vital for future research on LINC complex function and cellular processes.