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Related Concept Videos

Membrane Carbohydrates01:30

Membrane Carbohydrates

The plasma membrane is a dynamic barrier composed of lipids, proteins, and carbohydrates. It is the epicenter of many cellular processes required for cell growth and survival. Carbohydrates have unique structural and chemical properties that help the plasma membrane to carry out its functions effectively.
Membrane carbohydrates do not have any hydrophobic region and are exclusively located on the cell's outer surface. The addition of sugar molecules or glycosylation of proteins happens in...
Protein Modifications in the RER01:26

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.
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
Glucose Transporters01:27

Glucose Transporters

Glucose transporters facilitate the transport of glucose across the cell membrane. In addition to glucose, some glucose transporters can also aid the movement of other hexoses such as fructose, mannose, and galactose.
Facilitated diffusion-glucose transporters (GLUTs) are encoded by the solute-linked carrier (SLC) family 2, subfamily A gene family, or SLC2A. The 14 GLUT protein members are distributed into three classes:
Structure and Function of Erythrocytes01:29

Structure and Function of Erythrocytes

There are between 4.2 and 6 million erythrocytes, also known as red blood cells, in every microliter of blood. These cells are small, flattened biconcave discs with centers that are depressed.
The erythrocyte plasma membrane is associated with proteins such as spectrin, which forms a flexible cytoplasmic meshwork. This meshwork allows erythrocytes to twist, turn, become cup-shaped, and regain their biconcave shape as they pass through narrow capillaries. Additionally, erythrocytes can form...
Lifecycle of Erythrocytes01:22

Lifecycle of Erythrocytes

Erythrocytes, also known as red blood cells, constantly move through blood capillaries. As a result, they damage their plasma membrane due to the continuous friction. Typically, after 100 to 120 days, erythrocytes become rigid and fragile as they wear out. As they pass through small vessels in the spleen and liver, they can get trapped and break apart into fragments.
The resident phagocytic macrophages deal with these damaged cells by engulfing them and separating their globin and heme groups.

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Glutamine Flux Imaging Using Genetically Encoded Sensors
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Published on: July 31, 2014

Ultrastructure of human erythrocyte GLUT1.

C Graybill1, A N van Hoek, D Desai

  • 1Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, Massachusetts 01606, USA.

Biochemistry
|June 28, 2006
PubMed
Summary

The glucose transporter GLUT1 likely exists as a tetrameric complex. Detergents influence GLUT1

Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Protein Research

Background:

  • The glucose transporter GLUT1 is crucial for cellular glucose uptake.
  • Understanding GLUT1's quaternary structure is key to its function.
  • Detergents are often used to study membrane proteins but can alter their structure.

Purpose of the Study:

  • To investigate the quaternary structure of the glucose transporter GLUT1.
  • To determine the influence of various detergents on GLUT1's aggregation state.
  • To explore the self-assembly properties of GLUT1 in lipid bilayers.

Main Methods:

  • Hydrodynamic size analysis of GLUT1/lipid/detergent micelles.
  • Electron microscopy of GLUT1 micelles and proteoliposomes.

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  • Freeze-fracture electron microscopy to visualize GLUT1 in lipid bilayers.

    • Main Results:

    • Evidence supports GLUT1 forming a multimeric, likely tetrameric, complex.
    • Detergents like octyl glucoside stabilize GLUT1 oligomers, while CHAPS and dodecyl maltoside promote dissociation.
    • GLUT1 self-associates within the lipid bilayer, and its quaternary structure can be modulated by detergent and lipid environments.

    Conclusions:

    • GLUT1 exists as a stable multimeric complex, predominantly tetrameric.
    • Specific detergents can either stabilize or destabilize GLUT1 quaternary structure.
    • GLUT1 exhibits self-association in lipid bilayers, suggesting dynamic structural regulation.