Reactome | NCAM1 trans-homophilic interaction

NCAM1 trans-homophilic interaction

Stable Identifier

R-RNO-420397

Type

Reaction [binding]

Species

Rattus norvegicus

Compartment

plasma membrane

ReviewStatus

5/5

General

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SVG | | PPTX | SBGN

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
14527396	Structure and interactions of NCAM Ig1-2-3 suggest a novel zipper mechanism for homophilic adhesion Kasper, C, Diederichs, K, Soroka, V, Welte, W, Poulsen, FM, Larsen, IK, Kiselyov, VV, Kastrup, JS, Kolkova, K, Berezin, V, Bock, E, Breed, J	Structure	2003
15662836	Zippers make signals: NCAM-mediated molecular interactions and signal transduction Walmod, PS, Kolkova, K, Berezin, V, Bock, E	Neurochem Res	2004