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Posttranslational modifications of GLUT4 affect its subcellular localization and translocation
Jessica B A Sadler1, Nia J Bryant, Gwyn W Gould
1Institute of Molecular, Cell and Systems Biology, Davidson Building, College of Medical Veterinary and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK. Cassie.Welburn@Glasgow.ac.uk.
International Journal of Molecular Sciences
|May 14, 2013
Summary
Posttranslational modifications regulate facilitative glucose transporter type 4 (GLUT4) trafficking. These modifications are crucial for GLUT4
Area of Science:
- Molecular biology
- Cellular physiology
- Endocrinology
Background:
- Facilitative glucose transporter type 4 (GLUT4) is essential for glucose homeostasis in muscle and adipose tissue.
- GLUT4 primarily resides in intracellular compartments, with minimal presence at the plasma membrane without insulin stimulation.
- Insulin triggers GLUT4 translocation to the cell surface, enhancing glucose uptake.
Purpose of the Study:
- To review the impact of posttranslational modifications on GLUT4 function.
- To elucidate the role of posttranslational modifications in insulin-regulated GLUT4 trafficking.
Main Methods:
- Literature review of studies investigating GLUT4 trafficking and posttranslational modifications.
- Analysis of existing data on the molecular mechanisms governing GLUT4 localization and function.
Main Results:
- GLUT4 undergoes continuous trafficking through recycling endosomes, the trans Golgi network, and GLUT4-storage vesicles (GSVs).
- Insulin-sensitive mobilization of GLUT4 from GSVs to the plasma membrane is a key regulatory step.
- Multiple posttranslational modifications influence GLUT4's function and its regulated intracellular transport.
Conclusions:
- Posttranslational modifications are critical regulators of GLUT4's cellular localization and activity.
- Understanding these modifications provides insights into glucose metabolism and potential therapeutic targets for metabolic diseases.
Related Concept Videos
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.
01:27Post-translational Translocation of Proteins to the RER
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
01:26Protein 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.
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.
01:02Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
01:27Glucose 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:
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:
01:25Protein Glycosylation
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Glycosylation occurs in...