ArticleHuman cell2026
Matriptase proteolysis selectively drives disassembly and internalization of the claudin-7 complex while preserving E-cadherin.
Article in Human cell, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
Claudin-7 is a basolaterally enriched tight junction protein that participates in membrane complexes with EpCAM and Trop-2, linking epithelial adhesion to barrier organization. Although proteolytic processing of EpCAM/Trop-2 has been proposed to regulate this complex, its functional consequences for claudin-7 remain unresolved. Here, we define the role of matriptase in regulating claudin-7 dynamics in HaCaT human keratinocytes. Under steady-state conditions, matriptase knockout had only modest effects on claudin-7 distribution, suggesting a limited role in initial complex formation. In contrast, induction of matriptase autoactivation by mildly acidic stress triggered rapid and pronounced remodeling of claudin-7 complex in parental cells. Claudin-7 underwent progressive redistribution from continuous junctional staining to discontinuous bar-like structures, followed by the appearance of abundant intracellular puncta consistent with endocytosed vesicles, ultimately leading to its removal from the cell surface. This dynamic process was temporally coordinated and accompanied by increased accessibility of the claudin-7 C-terminus, indicating disassembly of claudin-7 complexes. These changes were abolished in matriptase-deficient cells, in which claudin-7 remained stably associated with cell-cell interfaces and failed to internalize. Suppression of matriptase autoactivation by NaCl similarly prevented claudin-7 internalization, demonstrating that proteolytic activity is required for this process. Notably, adherens junctions remained largely intact with E-cadherin continuously localized at cell-cell interfaces. Collectively, these findings establish that matriptase proteolytic activity is essential for disassembly and internalization of claudin-7 complex. This work supports a model in which the EpCAM/Trop-2-claudin-7 axis functions as a protease-regulated membrane complex that dynamically modulates epithelial organization.
Indexed as
Identifiers
42440028What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.