Related Experiment Video

Updated: Jul 9, 2025

In Vitro Differentiation Model of Human Normal Memory B Cells to Long-lived Plasma Cells
10:26

In Vitro Differentiation Model of Human Normal Memory B Cells to Long-lived Plasma Cells

Published on: January 20, 2019

12.2K

PML Body Biogenesis: A Delicate Balance of Interactions

Sergey A Silonov1, Eugene Y Smirnov1, Irina M Kuznetsova1

  • 1Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, St. Petersburg 194064, Russia.

International Journal of Molecular Sciences
|December 9, 2023
PubMed

Insights

Promyelocytic leukemia (PML) protein isoforms are key to forming PML bodies, crucial cellular structures. This review explores PML protein domains, modifications, and interactions, proposing a new model for PML body assembly.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • PML bodies are vital subnuclear structures involved in numerous cellular functions.
  • The promyelocytic leukemia (PML) protein, a member of the tripartite motif (TRIM) family, is a core component of PML bodies.
  • Multiple PML protein isoforms exist due to alternative splicing, influencing their function.

Purpose of the Study:

  • To review current literature on PML body formation mechanisms.
  • To elucidate the role of individual PML protein domains and post-translational modifications in assembly.
  • To highlight the contribution of polyvalent, non-specific interactions to PML body formation.

Main Methods:

  • Literature review and synthesis of existing research findings.
  • Analysis of the structural and functional properties of PML protein domains.
  • Examination of the impact of post-translational modifications on PML protein behavior.

Main Results:

  • PML protein isoforms exhibit distinct C-terminal regions affecting their interactions.
  • Specific domains and post-translational modifications of PML are critical for PML body assembly.
  • Polyvalent, non-specific interactions contribute significantly to the dynamic formation of PML bodies.

Conclusions:

  • PML protein structure, modifications, and interactions are central to PML body formation.
  • A novel hypothetical model for PML body assembly is proposed based on current evidence.
  • Further research is needed to fully understand the complex mechanisms of PML body biogenesis.
Keywords:
PML-bodiesSUMO/SIMTRIM domainbiomolecular condensatesintrinsically disordered proteinliquid–liquid phase separationmembraneless organelle

More Related Videos

Author Spotlight: Exploring the Role of Inflammation in the Co-occurrence of Primary Sjogren's Syndrome and Lung Adenocarcinoma10:21

Author Spotlight: Exploring the Role of Inflammation in the Co-occurrence of Primary Sjogren's Syndrome and Lung Adenocarcinoma

Published on: September 20, 2024

460
Visualization of Endogenous Mitophagy Complexes In Situ in Human Pancreatic Beta Cells Utilizing Proximity Ligation Assay08:40

Visualization of Endogenous Mitophagy Complexes In Situ in Human Pancreatic Beta Cells Utilizing Proximity Ligation Assay

Published on: May 2, 2019

5.9K

Related Concept Videos

Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
3.5K
Abnormal Proliferation02:23

Abnormal Proliferation

Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the...
4.5K
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
7.4K
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
6.3K
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
8.5K
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.5K