NCAM1 trans-homophilic interaction

Stable Identifier
R-RNO-420397
Type
Reaction [binding]
Species
Rattus norvegicus
Compartment
General
SVG |   | PPTX  | SBGN
NCAM1 trans-homophilic interaction

Antiparallel NCAM interactions involve trans-interactions of NCAM molecules on opposed cell membranes. Based on structural and functional studies a 'double zipper' model has been proposed to describe these interactions. The first model - the 'flat zipper'- formed between NCAM1 cis-dimers from one cell surface interacting in trans through IgII-IgIII contacts with NCAM1 cis-dimers from another cell surface. The second model - the 'compact zipper'- is formed between NCAM1 cis-dimers from one cell surface interacting in trans through IgI-IgIII and IgII-IgII contacts with cis-dimers from another cell surface.

Abrogation of cis-dimerization inhibits NCAM mediated neurite outgrowth, and cis-dimerization of NCAM1 may be a necessary prerequisite for subsequent trans-interactions.

Literature References
PubMed ID Title Journal Year
15662836 Zippers make signals: NCAM-mediated molecular interactions and signal transduction

Walmod, PS, Kolkova, K, Berezin, V, Bock, E

Neurochem Res 2004
14527396 Structure and interactions of NCAM Ig1-2-3 suggest a novel zipper mechanism for homophilic adhesion

Soroka, V, Kolkova, K, Kastrup, JS, Diederichs, K, Breed, J, Kiselyov, VV, Poulsen, FM, Larsen, IK, Welte, W, Berezin, V, Bock, E, Kasper, C

Structure 2003
Participants
Orthologous Events
Authored
Reviewed
Created