Abstract
Syndecan-1 is a cell surface proteoglycan that can organize co-receptors into a multimeric complex to transduce intracellular signals. The syndecan-1 core protein has multiple domains that confer distinct cell- and tissue-specific functions. Indeed, the extracellular, transmembrane, and cytoplasmic domains have all been found to regulate specific cellular processes. Our previous work demonstrated that syndecan-1 controls lung epithelial migration and adhesion. Here, we identified the necessary domains of the syndecan-1 core protein that modulate its function in lung epithelial repair. We found that the syndecan-1 transmembrane domain has a regulatory function in controlling focal adhesion disassembly, which in turn controls cell migration speed. In contrast, the extracellular domain facilitates cell adhesion through affinity modulation of α(2)β(1) integrin. These findings highlight the fact that syndecan-1 is a multidimensional cell surface receptor that has several regulatory domains to control various biological processes. In particular, the lung epithelium requires the syndecan-1 transmembrane domain to govern cell migration and is independent from its ability to control cell adhesion via the extracellular domain.
Highlights
Syndecan-1 regulates migration and adhesion in the lung epithelium
We found that the syndecan-1 transmembrane domain has a regulatory function in controlling focal adhesion disassembly, which in turn controls cell migration speed
We demonstrate that the syndecan-1 extracellular domain controls cell adhesion through ␣21 integrin affinity modulation
Summary
Syndecan-1 regulates migration and adhesion in the lung epithelium. Results: The transmembrane domain modulates focal adhesion disassembly, whereas the extracellular domain regulates cell adhesion. Conclusion: Lung epithelial migration is governed by the syndecan-1 transmembrane domain and is independent of the extracellular domain control of cell adhesion. The syndecan-1 core protein has multiple domains that confer distinct cell- and tissue-specific functions. We found that the syndecan-1 transmembrane domain has a regulatory function in controlling focal adhesion disassembly, which in turn controls cell migration speed. The extracellular domain facilitates cell adhesion through affinity modulation of ␣21 integrin These findings highlight the fact that syndecan-1 is a multidimensional cell surface receptor that has several regulatory domains to control various biological processes. The lung epithelium requires the syndecan-1 transmembrane domain to govern cell migration and is independent from its ability to control cell adhesion via the extracellular domain. We demonstrate that the syndecan-1 extracellular domain controls cell adhesion through ␣21 integrin affinity modulation. The extracellular domain by itself has no effect on cell migration and requires the transmembrane domain to control migration speed and focal adhesion disassembly
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