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Updated: Jul 19, 2026

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Published on: February 21, 2016
Mammalian lin-7 stabilizes polarity protein complexes
Samuel W Straight1, Jay N Pieczynski, Eileen L Whiteman
1Department of Internal Medicine, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.
Mammalian Lin-7 protein is crucial for maintaining tight junctions in epithelial cells. Its absence leads to PALS1 protein instability, disrupting cell polarity and barrier function.
Area of Science:
- Cell Biology
- Epithelial Biology
- Protein Interactions
Background:
- Mammalian Lin-7 protein complexes are involved in determining epithelial cell polarity.
- Lin-7 interacts with proteins like PALS1, crucial for cell structure and function.
Purpose of the Study:
- To investigate the role of Lin-7 in maintaining tight junction formation and protein stability in polarized epithelial cells.
- To identify the specific domains of Lin-7 and its binding partners essential for its function.
Main Methods:
- Utilized small hairpin RNA (shRNA) to knock down Lin-7 expression in Madin-Darby canine kidney II cells.
- Assessed tight junction integrity via transepithelial electrical resistance (TEER) measurements and ZO-1 protein localization.
- Performed rescue experiments using exogenous expression of Lin-7 constructs and PALS1.
Main Results:
- Lin-7 knockdown caused defects in tight junction formation, indicated by reduced TEER and ZO-1 mislocalization.
- Loss of Lin-7 led to decreased expression of binding partners PALS1 and PATJ.
- Exogenous expression of Lin-7's L27 domain or PALS1 rescued the observed defects, restoring PATJ levels.
- Lin-7 knockdown resulted in PALS1 protein instability and increased degradation.
Conclusions:
- Mammalian Lin-7 stabilizes PALS1 protein, which is essential for maintaining tight junction integrity in epithelial cells.
- Lin-7's L27 domain is critical for its function in stabilizing PALS1 and preserving cell polarity.
- Lin-7 plays a vital role in epithelial barrier function through PALS1 stabilization.
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