Human Caspr2 was cloned, while endogenous rat brain localization and biochemical assays showed juxtaparanodal enrichment and Kv1.2/Kvβ2-associated complexes. Reconstitution with only the tested channel subunits did not yield a stable complex, and occasional outermost glial paranodal loops were labeled.

The paper defines the large human CNTNAP2 genomic locus and its predicted Caspr2 protein architecture. The available abstract does not establish an experimentally performed nerve-impulse transmission step.

Human association and fetal-expression analyses relate CNTNAP2 to autism/language context. Regional fetal RNA distribution, childhood first-word measures and reported recessive regression do not separately demonstrate regional developmental participation or adult behavior.

Mouse limbic and human temporal-cortex expression are distinct observations. Rat P9 brain fractionation supports a synaptic plasma-membrane pool, while human variant association remains limited by segregation and population context.

FOXP2 binds and regulates CNTNAP2 in human neuronal cells; fetal cortical expression and language-associated variation connect the genes biologically. The assayed DNA-regulatory step is performed by FOXP2, not evidence by itself of CNTNAP2-driven cortical development.

The complete abstract reports Caspr2–carboxypeptidase E association by two-hybrid, GST pull-down and co-immunoprecipitation, with neuronal and transfected-cell colocalization. These data support positive protease binding without establishing catalytic regulation.

Human HA-tagged Caspr2 in rat hippocampal neurons reaches the axonal surface through selective somatodendritic endocytosis. Tail and motif manipulations, surface labeling and early-endosomal observations distinguish trafficking pools from polarized surface residence.

Human biallelic CNTNAP2 defects cause severe neurodevelopmental disease with speech impairment and variable autistic features. Separate Drosophila neurexin-IV experiments concern synaptic organization; speech loss in patients is not an imitation-learning assay.

HI-II-14 provides positive human CNTNAP2–MEOX2 pair records with validated, array and pooling two-hybrid evidence. General orthogonal validation of the map is not claimed as an additional exact-pair assay.

Human CASPR2 ectodomain binds CNTN1 directly in biolayer interferometry and in cell-surface assays. Purified contactin-family comparisons were negative for other tested contactins under those conditions, which does not erase positive CNTN2 results obtained with different presentations.

Mouse Cntnap2 loss and human CNTNAP2 rescue alter PV expression and interneuron maturation/physiology. MGE proliferation and survival were reported unchanged, and fate-mapped interneuron numbers were normal.

HuRI supports the positive CNTNAP2–POLR2G and CNTNAP2–GORASP2 pairs. The screen records do not themselves locate an interface or demonstrate a native transcriptional or Golgi function for CNTNAP2.

Human CNTNAP2 transgenes rescue junction morphology and locomotion in nlr-1-deficient worms and restore Cx43-based junction assembly. The direct actin-binding experiments are on worm NLR-1 and are not relabeled as human CNTNAP2 biochemical measurements.

Quantitative holdup assays directly test the human CNTNAP2 terminal peptide against isolated human PDZ domains. Positive records define the binding class without establishing all full-length cellular complexes or their physiological importance.

Mouse Caspr2 loss redistributes juxtaparanodal Kv1 channels without lowering total Kv1.2. Rat brain and transfected-cell association with TAG-1 supports a structural complex; the experiments do not completely distinguish initial recruitment from maintenance.

Human Caspr2-Fc and TAG-1 constructs support presentation-dependent binding in transfected cells and rodent neurons. Endogenous rat neuronal labeling identifies presynaptic and glutamatergic/GABAergic sites, with effects on inhibitory contacts.

The complete abstract reports that the Caspr2 cytoplasmic region is required for juxtaparanodal organization, whereas removal of the terminal PDZ-binding sequence still permits rescue. PSD93/PSD95 loss does not abolish the Caspr2–Kv1 complex.

Mouse Caspr/Caspr2 double-mutant experiments support axonal domain organization. The abstract explicitly reports Caspr2 at paranodes in Caspr-deficient nerves, without restoration of a distinct paranodal junction.

Cntnap2-deficient rats show altered acoustic startle and progressively impaired prepulse inhibition, accompanied by auditory timing changes. These support organismal circuit context rather than an independent molecular activity.

Mouse DRG antibody and genetic-context experiments support Caspr2 participation in CD24-dependent neurite responses. The source uses Caspr1 knockout and explicitly lacks Caspr2-null neurons; these experiments are not renamed Caspr2 knockouts.