Reactome | L1 linked to actin cytoskeleton by ankyrin

L1 linked to actin cytoskeleton by ankyrin

Stable Identifier

R-HSA-392751

Type

Reaction [binding]

Species

Homo sapiens

Compartment

cytosol, plasma membrane

ReviewStatus

5/5

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L1 linked to actin cytoskeleton by ankyrin

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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 Needham, LK, Thelen, K, Maness, PF	J Neurosci	2001
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