Related Experiment Video

Updated: Mar 20, 2026

Modeling Myotonic Dystrophy 1 in C2C12 Myoblast Cells
09:39

Modeling Myotonic Dystrophy 1 in C2C12 Myoblast Cells

Published on: July 29, 2016

16.1K

UBE2B is implicated in myofibrillar protein loss in catabolic C2C12 myotubes

Cécile Polge1, Roza Leulmi1, Marianne Jarzaguet1

  • 1INRA, UMR 1019, UNH, CRNH Auvergne Saint Genès Champanelle F-63122 France; Clermont Université, Université d'Auvergne, Unité de Nutrition Humaine BP 10448 Clermont-Ferrand F-63000 France.

Journal of Cachexia, Sarcopenia and Muscle
|May 31, 2016
PubMed
Abstract

Keywords:
C2C12 myotubesE2 Ubiquitin‐conjugating enzymeE3 ligaseUbiquitinUbiquitin proteasome system

More Related Videos

Methods to Assess Subcellular Compartments of Muscle in C. elegans10:13

Methods to Assess Subcellular Compartments of Muscle in C. elegans

Published on: November 13, 2014

17.3K
Bioenergetic Profile Experiment using C2C12 Myoblast Cells07:20

Bioenergetic Profile Experiment using C2C12 Myoblast Cells

Published on: December 6, 2010

51.5K

Related Concept Videos

Cross-bridge Cycle01:26

Cross-bridge Cycle

As muscle contracts, the overlap between the thin and thick filaments increases, decreasing the length of the sarcomere—the contractile unit of the muscle—using energy in the form of ATP. At the molecular level, this is a cyclic, multistep process that involves binding and hydrolysis of ATP, and movement of actin by myosin.
124.5K
Formation of Muscle Fibers from Myoblasts01:13

Formation of Muscle Fibers from Myoblasts

De novo myogenesis, or the formation of muscle fibers, begins during the early embryonic stages. The skeletal muscle is formed from somites– blocks of embryonic cell layers. The somites are further divided into dermatomes, myotomes, sclerotomes, and syndetomes. Among these, the myotomes give rise to muscle fibers.
Muscle progenitor cells (MPCs) are formed from the myotomes. MPCs express genes that encode the transcription factors Pax3 and Pax7. Along with Pax 3/7, other transcription...
6.7K
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
6.7K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
5.4K
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
2.0K