Sortilin-glut4 Interaction
Sortilin-glut4 Interaction - Related Videos
03:38
Imaging GLUT4 Protein Trafficking in Mouse Primary Hypothalamic Neurons Using Deconvolution Microscopy
0 Views •
2025
Source: Changou, C. A., et. al. Live Images of GLUT4 Protein Trafficking in Mouse Primary Hypothalamic Neurons Using Deconvolution Microscopy. J. Vis. Exp. (2017).This video showcases the imaging of insulin-induced GLUT4 translocation in hypothalamic neurons, employing deconvolution microscopy to capture and analyze GFP-GLUT4 trafficking dynamics with high resolution.
05:39
Quantitative Measurement of GLUT4 Translocation to the Plasma Membrane by Flow Cytometry
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Cited by 20 •
2010
This protocol describes a rapid technique to quantify the translocation of GLUT4 from the cytoplasm to the plasma membrane of cells by flow cytometry.
08:47
Live Images of GLUT4 Protein Trafficking in Mouse Primary Hypothalamic Neurons Using Deconvolution Microscopy
0 Views •
Cited by 8 •
2017
This protocol describes a technique for observation of real-time Green Fluorescence Protein (GFP) tagged Glucose Transporter 4 (GLUT4) protein trafficking upon insulin stimulation and characterization of the biological role of CCR5 in the insulin–GLUT4 signaling pathway with Deconvolution Microscopy.
06:41
Assessment of Social Interaction Behaviors
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Cited by 561 •
2011
Here we describe a detailed protocol for examination of sociability in mice by using Crawley's sociability and preference for social novelty test. We describe the advantages and possible applications for this procedure, including critical details important for correct interpretation of the results.
05:48
3D Co-culture with Direct Interaction: Co-culturing Cancer Cells with Monocytes to Study Their Interaction
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2023
This video describes the 3D co-culture of breast cancer cells with monocytes to study their interaction in an extracellular matrix extract (ECME) based environment. This method helps in studying specific features such as collagen degradation, immune cell recruitment, and cell invasion.
FAQs
Sortilin contributes to GLUT4 routing as an intracellular sorting receptor. It helps direct the transporter through trans-Golgi and endosomal compartments into specialized storage vesicles. This pathway places GLUT4 in a regulated intracellular pool rather than continuously at the plasma membrane. In biochemical terms, the interaction links protein sorting with later control of transporter availability and glucose uptake.
After insulin signaling, GLUT4-containing storage vesicles move toward the plasma membrane and fuse with it, increasing glucose transport into cells. This response shows that sorting and insulin-dependent delivery are connected but distinct stages. Sortilin helps establish the intracellular route, whereas insulin signaling regulates when the stored transporter becomes available at the cell surface.
The interaction connects intracellular protein trafficking with cellular glucose uptake and energy metabolism. Proper GLUT4 sorting allows the transporter to enter a storage pathway from which it can later be delivered to the plasma membrane after insulin signaling. Studying this connection helps explain how compartment organization contributes to glucose balance rather than viewing transport as an isolated membrane event.
Sorting occurs when sortilin helps route GLUT4 through trans-Golgi and endosomal compartments into storage vesicles. Delivery is a later event in which insulin signaling promotes vesicle movement and fusion with the plasma membrane. Separating these stages helps researchers determine whether abnormal glucose transport reflects faulty intracellular routing, impaired mobilization, or a problem with final membrane delivery.
Studying this association can help researchers examine whether altered intracellular trafficking is linked to impaired GLUT4 delivery and reduced insulin-responsive glucose transport. Its value lies in connecting a molecular interaction with a cellular outcome, providing context for defects associated with insulin resistance rather than treating reduced glucose uptake as an isolated transport problem.
The sortilin-GLUT4 interaction provides a biochemical framework for linking defects in intracellular GLUT4 handling with impaired cellular glucose uptake. It does not describe disease by itself; instead, it identifies trafficking and insulin-responsive membrane delivery as processes whose disruption may help explain abnormal glucose homeostasis in type 2 diabetes and related metabolic disorders.