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Role of adaptin protein complexes in intracellular trafficking and their impact on diseases
- Source :
- Bioengineered, article-version (VoR) Version of Record, Bioengineered, Vol 12, Iss 1, Pp 8259-8278 (2021)
- Publication Year :
- 2021
- Publisher :
- Taylor & Francis, 2021.
-
Abstract
- Adaptin proteins (APs) play a crucial role in intracellular cell trafficking. The ‘classical’ role of APs is carried out by AP1‒3, which bind to clathrin, cargo, and accessory proteins. Accordingly, AP1–3 are crucial for both vesicle formation and sorting. All APs consist of four subunits that are indispensable for their functions. In fact, based on studies using cells, model organism knockdown/knock-out, and human variants, each subunit plays crucial roles and contributes to the specificity of each AP. These studies also revealed that the sorting and intracellular trafficking function of AP can exert varying effects on pathology by controlling features such as cell development, signal transduction related to the apoptosis and proliferation pathways in cancer cells, organelle integrity, receptor presentation, and viral infection. Although the roles and functions of AP1‒3 are relatively well studied, the functions of the less abundant and more recently identified APs, AP4 and AP5, are still to be investigated. Further studies on these APs may enable a better understanding and targeting of specific diseases. APs known or suggested locations and functions.<br />GRAPHICAL ABSTRACT
- Subjects :
- Cellular pathology
intracellular trafficking
Protein subunit
Reviews
Bioengineering
Apoptosis
Review
Applied Microbiology and Biotechnology
Clathrin
clathrin
Organelle
virus infection
cancer
Humans
Cell Proliferation
biology
Cell growth
Adaptin protein
Biological Transport
General Medicine
cellular pathology
Cell biology
Adaptor Proteins, Vesicular Transport
cargo protein
Cancer cell
biology.protein
Signal transduction
Intracellular
TP248.13-248.65
Biotechnology
Signal Transduction
Subjects
Details
- Language :
- English
- ISSN :
- 21655987 and 21655979
- Volume :
- 12
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Bioengineered
- Accession number :
- edsair.doi.dedup.....6e347c506348d1d2e1752e7e4b463bfd