L1 dimer binds Ankyrin

Stable Identifier
Reaction [binding]
Homo sapiens
SVG |   | PPTX  | SBGN
L1 dimer binds Ankyrin

L1 recruits membrane skeletal component ankyrin to cell to cell contact sites in response to cis interaction with homophilic axonin 1/TAG 1 or trans L1 L1 homophilic interaction although in mammalian cells trans binding interactions are not required. L1 interacts with ankyrin proteins through two highly conserved amino acid sequence motifs, LADY and FIGQY.
Ankyrin binding immobilizes L1 molecules in the neuronal plasma membrane. This interaction is required for axon maintenance. L1 also elevates cyclic AMP levels in neurons via ankyrin B and mediates Ca+2 dependent attraction.The L1/ankyrin interaction is a vital determinant of synaptic targeting of retinal axons to the superior colliculus and cooperates with EphrinB/EphB signaling to induce axon branch attraction.

Literature References
PubMed ID Title Journal Year
19110015 The cell adhesion molecule L1 controls growth cone navigation via ankyrin(B)-dependent modulation of cyclic AMP

Ooashi, N, Kamiguchi, H

Neurosci Res 2009
9837910 Cis-activation of L1-mediated ankyrin recruitment by TAG-1 homophilic cell adhesion

Malhotra, JD, Tsiotra, P, Karagogeos, D, Hortsch, M

J Biol Chem 1998
12925712 Ankyrin binding mediates L1CAM interactions with static components of the cytoskeleton and inhibits retrograde movement of L1CAM on the cell surface

Gil, OD, Sakurai, T, Bradley, AE, Fink, MY, Cassella, MR, Kuo, JA, Felsenfeld, DP

J Cell Biol 2003
11222639 Cytoplasmic domain mutations of the L1 cell adhesion molecule reduce L1-ankyrin interactions

Needham, LK, Thelen, K, Maness, PF

J Neurosci 2001
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