L1 linked to actin cytoskeleton by ankyrin

Stable Identifier
Reaction [binding]
Homo sapiens
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Ankyrins are bifunctional linker proteins that tether L1 to the membrane associated, spectrin based actin cytoskeleton. Spectrin is a tetramer of two alpha- and two beta-chains. The spectrin alpha chain has 21 and the beta chain has 16 (conventional beta) or 30 (heavy beta) successive triple helix repeats. At the N-terminus of beta spectrin, there is a pair of CH (calponin homology) domains which together form an actin binding domain, while the triple helical repeats 14-15 bind ankyrin.
Interaction with spectrin bound F-actin blocks the mobility of L1 and this immobilization mediates adjacent neuron adhesions.

Literature References
PubMed ID Title Journal Year
16904324 Phosphorylation of L1-type cell-adhesion molecules--ankyrins away!

Nagaraj, K, Hortsch, M

Trends Biochem Sci 2006
11222639 Cytoplasmic domain mutations of the L1 cell adhesion molecule reduce L1-ankyrin interactions

Thelen, K, Needham, LK, Maness, PF

J Neurosci 2001
17223356 betaIV-spectrin forms a diffusion barrier against L1CAM at the axon initial segment

Komada, M, Kamiguchi, H, Nishimura, K, Akiyama, H

Mol Cell Neurosci 2007
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