Related Experiment Video
Updated: Jul 19, 2026
12:26
Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
Menin and its interacting proteins: elucidation of menin function
Katalin Balogh1, Károly Rácz, Attila Patócs
1Second Department of Medicine, Semmelweis University, Szentkirályi str. 46, H-1088 Budapest, Hungary. bkatus@freemail.hu
Trends in Endocrinology and Metabolism: TEM
|September 26, 2006
Summary
The MEN1 gene
Area of Science:
- Genetics
- Molecular Biology
- Oncology
Background:
- The MEN1 gene encodes the tumor suppressor protein menin.
- Mutations in the MEN1 gene cause Multiple Endocrine Neoplasia type 1 (MEN 1) syndrome.
- The precise intracellular functions of menin remain incompletely understood.
Purpose of the Study:
- To elucidate the intracellular functions of the menin protein.
- To investigate the role of menin-protein interactions in physiological processes.
- To explore the potential contribution of disrupted menin interactions to MEN 1 syndrome pathogenesis.
Main Methods:
- Literature review of recent data on menin and its interacting proteins.
- Analysis of proposed roles in cell growth regulation.
- Examination of involvement in cell cycle control and genome stability.
Main Results:
- Menin interacts with other proteins, influencing cell growth and cell cycle control.
- These interactions are potentially crucial for genome stability.
- Menin's interactions may play a role in bone development and stem cell differentiation.
Conclusions:
- Menin's interactions with other proteins are vital for normal cellular functions.
- Dysregulation of these interactions could be a key factor in the development of MEN 1 syndrome.
- Further research into menin-protein interactions is warranted for understanding MEN 1.
More Related Videos
10:36Identifying Protein-protein Interaction in Drosophila Adult Heads by Tandem Affinity Purification (TAP)
Published on: December 5, 2013
10:05Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay
Published on: January 16, 2017
Related Concept Videos
02:26Protein Networks
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
02:04Protein-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 polypeptide...
01:26Tension Response at Adherens Junctions
The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
01:22PI3K/mTOR/AKT Signaling Pathway
The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast, mTORC2 consists of a rapamycin-insensitive companion...
01:58Mechanical Protein Function
Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force.