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CNTNAP1 mutations were found to induce characteristic ultrastructural lesions of the paranodal region.
report a consanguineous Arab family from Qatar with three children having an early lethal form of arthrogryposis multiplex congenita and a novel frameshift mutation in CNTNAP1
Mutations in CNTNAP1 and ADCY6 (show ADCY6 Proteins) are responsible for severe arthrogryposis multiplex congenita with axoglial defects
VDAC1 (show VDAC1 Proteins) and CNTNAP1 associate with gamma-secretase in detergent-resistant membranes and affect amyloid precursor protein (show APP Proteins) processing.
Simultaneous deletion of Caspr and Caspr2 (show CNTNAP2 Proteins) disrupts the internodal organization of Kv1.2 (show KCNA2 Proteins).
Caspr co-localizes and interacts with APP (show APP Proteins). Amyloid-beta (Abeta (show APP Proteins)) 40 and Abeta42 generation were also reduced in HEK (show EPHA3 Proteins)-APP (show APP Proteins) cells by Caspr overexpression.
Caspr labeling was observed through much of the retina, including horizontal, bipolar, amacrine, and ganglion cells.
Clustering of Caspr at initial contact sites between OL processes and the axon requires glial expression of NF155 but not of contactin. Expression of membrane proteins along the axolemma is determined by the type of the contacting glial cells.
These results suggest that Caspr serves as a "transmembrane scaffold" that stabilizes the Caspr/contactin adhesion complex at the paranodal junction by connecting it to cytoskeletal components within the axon.
F3/contactin and caspr/paranodin traffic to the cell surface via a non-conventional pathway
Nogo-A (show RTN4 Proteins) interacts in trans with axonal Caspr at CNS paranodes, an interaction that may have a role in modulating axon-glial junction architecture and possibly K(+)-channel (show KCNC4 Proteins) localization during development.
the Caspr/Cont complex is essential for the formation of axoglial SJ
Caspr protein is required for recruitment and retention of KCNQ4 (show KCNQ4 Proteins) at calyceal synapses in vestibular hair cells.
The Caspr gene has been identified in the neurological mutant shambling (shm) mouse and shown to encode the contactin-associated protein, which is a major component of the paranodal junction in myelinated nerves.
The gene product was initially identified as a 190-kD protein associated with the contactin-PTPRZ1 complex. The 1,384-amino acid protein, also designated p190 or CASPR for 'contactin-associated protein,' includes an extracellular domain with several putative protein-protein interaction domains, a putative transmembrane domain, and a 74-amino acid cytoplasmic domain. Northern blot analysis showed that the gene is transcribed predominantly in brain as a transcript of 6.2 kb, with weak expression in several other tissues tested. The architecture of its extracellular domain is similar to that of neurexins, and this protein may be the signaling subunit of contactin, enabling recruitment and activation of intracellular signaling pathways in neurons.
contactin associated protein 1
, contactin-associated protein 1-like
, contactin-associated protein 1
, neurexin 4
, neurexin IV
, neurexin 4 (contactin associated protein)