4.7 Article

The interaction between L1-type proteins and ankyrins - a master switch for L1-type CAM function

Journal

CELLULAR & MOLECULAR BIOLOGY LETTERS
Volume 14, Issue 1, Pages 57-69

Publisher

BMC
DOI: 10.2478/s11658-008-0035-4

Keywords

Cell adhesion; Ankyrins; Membrane skeleton; Tyrosine phosphorylation; Neurite outgrowth; Neuromuscular junction; Synapse; Synaptogenesis; Drosophila

Funding

  1. University of Michigan
  2. [RO1 HD050725-01A1]

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L1-type cell adhesion molecules (CAMs) are important mediators of neural differentiation, including axonal outgrowth and pathfinding and also of synapse formation and maintenance. In addition, their interactions with cytoskeletal components are highly conserved and regulated. How these different aspects of CAM functionality relate to each other is not well understood. Based on results from our and other laboratories we propose that ankyrin-binding to L1-type CAMs provides a master switch. The interaction with ankyrins directs L1-type adhesive proteins into different functional contexts, either ankyrin-independent functions, such as neurite outgrowth and axonal pathfinding or into ankyrin-dependent functions, such as L1's role at axon initial segments (AIS), paranodal regions, synapses and in dendrites.

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