Methods for Detecting Phosphorylated Proteins and Observing Intracellular Localization During Mitosis.

This protocol describes the detection of phosphorylated proteins within cells and the identification of their intracellular localization, with a particular focus on mitotic cells. While the detection of phosphorylated proteins can be achieved using radioactive labeling with Pi, this method presents experimental challenges due to the requirement for radioisotopes. Alternatively, detection using phosphorylation-specific antibodies is a potent method; however, it necessitates the identification of phosphorylation sites and further requires the generation of antibodies targeting these sites, making it effective only for thoroughly analyzed phosphorylations.

Efficacy of belt electrode skeletal muscle electrical stimulation on muscle flexibility of lower limbs: A randomized controlled pilot trial.

Background: Muscular contracture may be caused by immobility-induced muscle atrophy and skeletal muscle hypoxia. Belt electrode skeletal muscle electrical stimulation (B-SES) is a new type of neuromuscular electrical stimulation that can simultaneously contract the lower limb muscle groups, in contrast to the conventional pad-type electrodes. B-SES can suppress muscular atrophy and relieve hypoxia of the skeletal muscle and is considered an appropriate strategy for preventing muscular contracture.

Mitotic ER Exit Site Disassembly and Reassembly Are Regulated by the Phosphorylation Status of TANGO1.

Golgi fragmentation and ER exit site disassembly are considered to be the leading causes of the mitotic block of secretion from the ER. Although the mechanisms of Golgi fragmentation have been extensively characterized, ER exit block early in mitosis is not well understood. We previously demonstrated that TANGO1 organizes ER exit sites by directly interacting with Sec16.

COPII proteins exhibit distinct subdomains within each ER exit site for executing their functions.

Secretory proteins are exported from special domains of the endoplasmic reticulum (ER) termed ER exit sites, via COPII-coated carriers. We recently showed that TANGO1 and Sec16 cooperatively organize mammalian ER exit sites for efficient secretion. However, the detailed spatial organization of mammalian ER exit sites is yet to be revealed.