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Structural Characteristics, Binding Partners and Related Diseases of the Calponin Homology (CH) Domain
- Source :
- Frontiers in Cell and Developmental Biology, Vol 8 (2020), Frontiers in Cell and Developmental Biology
- Publication Year :
- 2020
- Publisher :
- Frontiers Media S.A., 2020.
-
Abstract
- The calponin homology (CH) domain is one of the most common modules in various actin-binding proteins and is characterized by an α-helical fold. The CH domain plays important regulatory roles in both cytoskeletal dynamics and signaling. The CH domain is required for stability and organization of the actin cytoskeleton, calcium mobilization and activation of downstream pathways. The CH domain has recently garnered increased attention due to its importance in the onset of different diseases, such as cancers and asthma. However, many roles of the CH domain in various protein functions and corresponding diseases are still unclear. Here, we review current knowledge about the structural features, interactome and related diseases of the CH domain.
- Subjects :
- 0301 basic medicine
calmodulin
actin cytoskeleton
Calmodulin
Mini Review
Calponin
Interactome
Homology (biology)
tropomyosin
03 medical and health sciences
Cell and Developmental Biology
0302 clinical medicine
transgelin-2
CH-domain-containing proteins
cancer
Cytoskeleton
lcsh:QH301-705.5
α-helix
biology
Chemistry
Cell Biology
Actin cytoskeleton
Tropomyosin
Cell biology
030104 developmental biology
Tubulin
tubulin
lcsh:Biology (General)
030220 oncology & carcinogenesis
biology.protein
Developmental Biology
Subjects
Details
- Language :
- English
- Volume :
- 8
- Database :
- OpenAIRE
- Journal :
- Frontiers in Cell and Developmental Biology
- Accession number :
- edsair.doi.dedup.....7132ec379cee27095d054ae5bab7eb6d