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Details on Person L1 recruits membrane skeletal component ankyrin to cell to c...
| Class:Id | Summation:374644 |
|---|---|
| _displayName | L1 recruits membrane skeletal component ankyrin to cell to c... |
| _timestamp | 2010-03-16 17:38:35 |
| created | [InstanceEdit:374643] Garapati, P V, 2008-07-30 10:19:01 |
| literatureReference | [LiteratureReference:374423] Cytoplasmic domain mutations of the L1 cell adhesion molecule reduce L1-ankyrin interactions [LiteratureReference:549030] L1 interaction with ankyrin regulates mediolateral topography in the retinocollicular projection |
| modified | [InstanceEdit:392734] Garapati, P V, 2009-03-07 11:19:40 [InstanceEdit:443578] Garapati, P V, 2009-10-12 [InstanceEdit:444909] Garapati, P V, 2009-10-27 [InstanceEdit:447049] Garapati, P V, 2009-11-19 [InstanceEdit:549028] Garapati, P V, 2010-03-16 |
| text | 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. |
| (summation) | [Reaction:374675] L1 dimer binds Ankyrin [Homo sapiens] [Reaction:443049] L1 dimer binds Ankyrin [Homo sapiens] |
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No pathways have been reviewed or authored by L1 recruits membrane skeletal component ankyrin to cell to c... (374644)
