Unknown

Dataset Information

0

Post-translational modification and regulation of actin.


ABSTRACT: Many of the best-studied actin regulatory proteins use non-covalent means to modulate the properties of actin. Yet, actin is also susceptible to covalent modifications of its amino acids. Recent work is increasingly revealing that actin processing and its covalent modifications regulate important cellular events. In addition, numerous pathogens express enzymes that specifically use actin as a substrate to regulate their hosts' cells. Actin post-translational alterations have been linked to different normal and disease processes and the effects associated with metabolic and environmental stressors. Herein, we highlight specific co-translational and post-translational modifications of actin and discuss the current understanding of the role that these modifications play in regulating actin.

SUBMITTER: Terman JR 

PROVIDER: S-EPMC3578039 | biostudies-literature | 2013 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Post-translational modification and regulation of actin.

Terman Jonathan R JR   Kashina Anna A  

Current opinion in cell biology 20121127 1


Many of the best-studied actin regulatory proteins use non-covalent means to modulate the properties of actin. Yet, actin is also susceptible to covalent modifications of its amino acids. Recent work is increasingly revealing that actin processing and its covalent modifications regulate important cellular events. In addition, numerous pathogens express enzymes that specifically use actin as a substrate to regulate their hosts' cells. Actin post-translational alterations have been linked to diffe  ...[more]

Similar Datasets

| S-EPMC5387672 | biostudies-literature
2020-08-26 | GSE156817 | GEO
| S-EPMC7320668 | biostudies-literature
| S-EPMC1163086 | biostudies-other
| S-EPMC3349990 | biostudies-literature
| S-EPMC3919261 | biostudies-literature
| S-EPMC8342498 | biostudies-literature
| S-EPMC7664127 | biostudies-literature
| S-EPMC8920986 | biostudies-literature
| S-EPMC6272617 | biostudies-literature