Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Regulation of Nuclear Protein Sorting

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...

Directing Proteins to the Rough Endoplasmic Reticulum

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...

Protein Modifications in the RER

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

Regulation of the Unfolded Protein Response

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...

Assembly of Signaling Complexes

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

Single-Strand DNA Binding Proteins

Single-Strand DNA Binding Proteins

For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Modeling and Characterization of Intestinal Senescence Using Human Organoids: Insights Into the Epithelial to Mesenchymal Transition.

Journal of cellular physiology·2026

Same author

Organoid phenotypic screening identified glycyrrhizin that confers protection against tumor necrosis factor-induced cell death.

Stem cell reports·2026

Same author

LXR activation in skeletal muscle cells enhances differentiation and promotes protein synthesis.

American journal of physiology. Endocrinology and metabolism·2026

Same author

MCARE enhances SERCA1 activity in fast-twitch muscle to maintain calcium handling and muscle integrity.

Nature communications·2025

Same author

Inhibition of potassium chloride cotransporters impairs muscle contraction and induces atrophy in C2C12 myotubes.

Bioscience, biotechnology, and biochemistry·2025

Same author

Pre-Stenting Inflammatory Burden Index (IBI) as a Predictor of Survival and Postoperative Complications in Patients with Obstructive Colorectal Cancer.

Journal of the anus, rectum and colon·2025

Search research articles

Related Experiment Video

Updated: Jun 26, 2026

Analysis of SCAP N-glycosylation and Trafficking in Human Cells

Analysis of SCAP N-glycosylation and Trafficking in Human Cells

Published on: November 8, 2016

SREBPs: protein interaction and SREBPs.

Ryuichiro Sato¹

¹Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, Japan. aroysato@mail.ecc.u-tokyo.ac.jp

The FEBS Journal

|January 16, 2009

Summary

Sterol regulatory element-binding proteins (SREBPs) are crucial for cellular lipid homeostasis. This review details how protein interactions regulate SREBP activity and function.

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Sterol regulatory element-binding proteins (SREBPs) are essential transcription factors that control lipid metabolism.
SREBP activity is tightly regulated through multiple cellular mechanisms to maintain lipid homeostasis.

Purpose of the Study:

To review the diverse regulatory mechanisms governing SREBP activity.
To highlight the critical role of protein-protein interactions in SREBP regulation.

Main Methods:

Literature review of published research on SREBP regulation.
Analysis of various protein interactions impacting SREBP localization, processing, and activity.

Main Results:

SREBP regulation involves intricate control over intracellular localization.

More Related Videos

Quantitative Determination of De Novo Fatty Acid Synthesis in Brown Adipose Tissue Using Deuterium Oxide

Quantitative Determination of De Novo Fatty Acid Synthesis in Brown Adipose Tissue Using Deuterium Oxide

Published on: May 12, 2023

Related Experiment Videos

Last Updated: Jun 26, 2026

Analysis of SCAP N-glycosylation and Trafficking in Human Cells

Analysis of SCAP N-glycosylation and Trafficking in Human Cells

Published on: November 8, 2016

Quantitative Determination of De Novo Fatty Acid Synthesis in Brown Adipose Tissue Using Deuterium Oxide

Quantitative Determination of De Novo Fatty Acid Synthesis in Brown Adipose Tissue Using Deuterium Oxide

Published on: May 12, 2023

Protein processing, limited proteolysis, and post-translational modifications are key regulatory steps.

Interactions with associated proteins significantly modulate SREBP function.

Conclusions:

Protein interactions are central to the complex regulatory network of SREBPs.
Understanding these interactions is vital for comprehending lipid metabolism and developing therapeutic strategies.