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Related Concept Videos

Histone Modification02:32

Histone Modification

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
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Histone Variants at the Centromere02:30

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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
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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.
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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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The writer...
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Inheritance of Chromatin Structures03:17

Inheritance of Chromatin Structures

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Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying...
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Related Experiment Video

Updated: Jun 29, 2025

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
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Dynein Light Intermediate Chains Exhibit Different Arginine Methylation Patterns.

Weiwen Bu1, Jie Di1, Junkui Zhao1

  • 1Department of Genetics and Cell Biology, Haihe Laboratory of Cell Ecosystem, State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, Tianjin, China.

Journal of Clinical Laboratory Analysis
|March 25, 2024
PubMed
Summary
This summary is machine-generated.

Dynein motor protein subunit LIC2 is methylated at arginine 397 by PRMT1. This post-translational modification (PTM) offers insights into dynein transport regulation and disease relevance.

Keywords:
PRMT1arginine methylationdyneinlight intermediate chainmicrotubule

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In vitro Methylation Assay to Study Protein Arginine Methylation
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In vitro Methylation Assay to Study Protein Arginine Methylation

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Area of Science:

  • Cellular biology
  • Molecular mechanisms of protein function
  • Neuroscience and disease

Background:

  • The motor protein dynein facilitates retrograde transport along microtubules, interacting with various cargoes via adaptor proteins.
  • Dynein light intermediate chain subunits (LIC1 and LIC2) mediate these interactions, forming distinct complexes with unique and overlapping functions.

Purpose of the Study:

  • To investigate the post-translational modifications (PTMs) of dynein light intermediate chain subunits (LIC1 and LIC2).
  • To identify specific methylation sites on LIC2 and the enzymes responsible for these modifications.
  • To understand how PTMs regulate dynein function and their implications in disease.

Main Methods:

  • Bioinformatic analysis of LIC1 and LIC2 C-terminal domains (CTDs).
  • Immunoprecipitation and immunoblotting to assess LIC2 methylation status and associated proteins.
  • Site-directed mutagenesis to pinpoint specific methylation sites on LIC2.

Main Results:

  • LIC2 exhibits distinct PTMs compared to LIC1.
  • LIC2 is specifically methylated at arginine 397.
  • Protein arginine methyltransferase 1 (PRMT1) catalyzes the methylation of LIC2 at arginine 397.

Conclusions:

  • Distinct PTMs of LIC subunits provide a versatile mechanism for dynein-mediated cargo transport.
  • Understanding LIC2 PTMs, particularly methylation at R397, is crucial for elucidating dynein's role in disease.
  • This discovery deepens our understanding of dynein complex regulation through PTMs.