Dynamic property of intermediate filaments: Regulation by phosphorylation
β Scribed by Masaki Inagaki; Yoichiro Matsuoka; Kunio Tsujimura; Shoji Ando; Toshiya Tokui; Toshitada Takahashi; Naoyuki Inagaki
- Book ID
- 102758430
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 894 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0265-9247
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β¦ Synopsis
Site-specific phosphorylation of intermediate filament (IF) proteins on serine and threonine residues leads to alteration of the filament structure, in vitro and in vivo. Protein kinases involved in cell signaling and those activated in mitosis dynamically control spatial and temporal organization of intracellular IF phosphorylation. Thus, IF phosphorylation appears to be one of the most predominant strategies in coordinating intracellular organization of the IF Accepted
π SIMILAR VOLUMES
Intermediate filament (IF) proteins, in contrast to microtubules and microfilaments, are preferentially expressed in higher eukaryotes, are relatively insoluble, and are made up of a large and diverse family of proteins (reviewed in [1][2][3][4][5]). Aside from the nuclear lamins, members of the cyt
## Abstract The animal cell cytoskeleton consists of three interconnected filament systems: actinβcontaining microfilaments (MFs), microtubules (MTs), and the lesser known intermediate filaments (IFs). All IF proteins share a common tripartite domain structure and the ability to assemble into 8β12