Trans-bonded pairs of E-cadherin exhibit a remarkable hierarchy of mechanical strengths
Bibliographic record
Abstract
Classical cadherins are primary mediators of calcium-dependent cell interactions in multicellular organisms. Organized in five tandemly repeated E-cadherin (EC) modules, the extracellular segments of these membrane-spanning glycoproteins interact homophilically between opposing cells to create highly regulated patterns of attachment stabilized by cytoskeletal elements inside the cells. Despite many structural and functional studies, a significant controversy exists in regard to the organization of cadherin binding in adhesion sites. Supported by considerable evidence, perhaps the most widely held view is that opposing N-terminal EC1-EC2 (EC12) domains form a "zipper" of bonds. However, immobilized on two atomically smooth surfaces and pushed to adhesive contact, opposing cadherins become fully interdigitated and unbind through three discrete jumps comparable with domain dimensions when pulled apart. So the question remains as to whether mechanical adhesion strength emanates solely from interactions between the peripheral N-terminal domains or involves multiple overlapping domains. It is also unclear whether a primary adhesion complex is formed by a single opposing pair of cadherins or whether the complex involves a more complicated network of cis-bonded multimers. To address these questions, we used a special jump/ramp mode of force spectroscopy to test isolated pairwise interactions between recombinant fragments of ECs. Besides the formation of strong trans-bonded dimers, we find a remarkable hierarchy of rupture strengths for bonds between the full five-domain fragments that suggests multiple mechanical functions for cadherins, perhaps providing distinct properties needed for transient-specific recognition as well as stable tissue formation.
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How this classification was reachedexpand
Full frame machine prediction
Teacher imitationNot calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.
Distilled classifier scores by category (both heads)
| Category | Codex | Gemma |
|---|---|---|
| Metaresearch | 0.000 | 0.000 |
| Meta-epidemiology (narrow) | 0.000 | 0.000 |
| Meta-epidemiology (broad) | 0.000 | 0.000 |
| Bibliometrics | 0.000 | 0.000 |
| Science and technology studies | 0.000 | 0.000 |
| Scholarly communication | 0.000 | 0.000 |
| Open science | 0.000 | 0.000 |
| Research integrity | 0.000 | 0.000 |
| Insufficient payload (model declined to judge) | 0.001 | 0.000 |
Machine scores (provisional)
The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.
Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.
score_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from itClassification
machine, unvalidatedMachine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.
How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".