L1 linked to actin cytoskeleton by ankyrin

Stable Identifier
R-HSA-392751
Type
Reaction [binding]
Species
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
11222639 Cytoplasmic domain mutations of the L1 cell adhesion molecule reduce L1-ankyrin interactions

Needham, LK, Thelen, K, Maness, PF

J Neurosci 2001
16904324 Phosphorylation of L1-type cell-adhesion molecules--ankyrins away!

Nagaraj, K, Hortsch, M

Trends Biochem Sci 2006
17223356 betaIV-spectrin forms a diffusion barrier against L1CAM at the axon initial segment

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

Mol Cell Neurosci 2007
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