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Regulation of gap junctions by phosphorylation of connexins
Archives of Biochemistry and Biophysics
|May 23, 2001
Summary
Gap junctions, crucial for cell communication, are regulated by connexin phosphorylation. This process impacts various cellular functions, including channel gating and protein trafficking.
Area of Science:
- Cell Biology
- Molecular Biology
Background:
- Gap junctions facilitate intercellular communication by allowing the passage of small molecules.
- These junctions are vital for development, metabolism, and growth control in animal cells.
- Vertebrate gap junctions are formed by connexin proteins, which undergo post-translational modifications.
Purpose of the Study:
- To review the regulatory role of connexin phosphorylation in gap junctional communication.
- To explore how phosphorylation affects various connexin-related cellular processes.
Main Methods:
- Literature review of studies on connexin phosphorylation.
- Analysis of identified protein kinases targeting connexins (e.g., protein kinase C, mitogen-activated protein kinase, v-Src tyrosine protein kinase).
Main Results:
- Connexins are primarily phosphorylated on serine residues, but phosphotyrosine is also observed.
- Phosphorylation influences connexin trafficking, assembly, disassembly, degradation, and channel gating.
- Specific kinases like protein kinase C and mitogen-activated protein kinase regulate connexin phosphorylation.
Conclusions:
- Connexin phosphorylation is a key mechanism regulating gap junction function and intercellular communication.
- Understanding these phosphorylation events provides insights into diverse biological processes controlled by gap junctions.
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