Regulation of Skeletal Muscle Differentiation by a Rapamycin -Sensitive Signaling Pathway

To gain further insight into myogenic regulation of mTOR, the structure-function relationship of mTOR was examined by a series of truncation and deletion mutants. Strikingly, the results indicate that the C-terminal 1187 amino acids are sufficient for mTOR's myogenic function and the N-terminal half of the protein is completely dispensable. Both the FKBP 12-rapamycin binding domain (FRB) and the kinase domain are necessary for mTOR's myogenic function despite kinase activity being dispensable. These observations provide structural insights into the regulatory mechanisms of mTOR, possibly involving association with regulators, and warrant further investigation to identify the potential partner proteins critical in mTOR signaling during skeletal myogenesis.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Microbiology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Erbay, Ebru

Contributors dc:contributor

• Chen, Jie

• Biology, Cell

Language dc:language

eng

Identifier

(MiAaPQ)AAI3130911

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/86664