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Allosteric Proteins-ATCase

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Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...

Ligand Binding and Linkage

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

Allosteric Regulation

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...

Allosteric Regulation

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...

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Related Experiment Video

Updated: Jul 17, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

ALS2CL, a novel ALS2-interactor, modulates ALS2-mediated endosome dynamics.

Kyoko Suzuki-Utsunomiya¹, Shinji Hadano, Asako Otomo

¹Department of Molecular Neuroscience, The Institute of Medical Sciences, Tokai University, Kanagawa, Japan.

Biochemical and Biophysical Research Communications

|January 24, 2007

Summary

A novel ALS2 homolog, ALS2CL, interacts with ALS2, forming a complex that modulates endosome dynamics. This interaction suppresses ALS2-induced endosome enlargement, impacting motor neuron disease pathways.

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Last Updated: Jul 17, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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In vivo and in vitro Studies of Adaptor-clathrin Interaction

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

Area of Science:

Molecular Biology
Cell Biology
Neuroscience

Background:

Amyotrophic lateral sclerosis type 2 (ALS2) is linked to motor neuron diseases and regulates endosome dynamics via Rab5.
A novel ALS2 homolog, ALS2CL, shares homology with ALS2 and is investigated for its role in cellular processes.

Purpose of the Study:

To investigate the molecular features of ALS2CL.
To elucidate the functional relationship between ALS2CL and ALS2.
To understand ALS2CL's role in ALS2-mediated endosome dynamics.

Main Methods:

Investigated ALS2CL homo-dimerization and interaction with ALS2 oligomers.
Analyzed co-localization of overexpressed ALS2CL and ALS2 in cultured cells.
Assessed the effect of ALS2CL on ALS2-induced endosome enlargement and cellular phenotype.

Main Results:

ALS2CL forms homo-dimers and interacts with ALS2 oligomers, creating a large ALS2/ALS2CL heteromeric complex.
Overexpressed ALS2CL co-localizes with ALS2 on membranous compartments in cultured cells.
ALS2CL suppresses ALS2-induced endosome enlargement and induces a perinuclear tubulo-membranous phenotype, dependent on ALS2CL-ALS2 interaction.

Conclusions:

ALS2CL is a novel ALS2-interacting protein.
ALS2CL plays a role in modulating ALS2-mediated endosome dynamics.
The ALS2CL-ALS2 interaction is crucial for regulating endosome morphology and cellular phenotype.