Extracellular GAPDH binds to L1 and enhances neurite outgrowth

Tatjana Makhina, Gabriele Loers, Christian Schulze, Barbara Ueberle, Melitta Schachner, Ralf Kleene

Research output: Contribution to journalArticlepeer-review

41 Scopus citations


We have identified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a binding partner for the cell adhesion molecule L1. GAPDH binds to sites within the extracellular domain of L1, namely the immunoglobulin-like domains I-VI and the fibronectin type III homologous repeats 4-5. Extracellular GAPDH was detected at the cell surface of neuronal cells by surface biotinylation and immunocytochemistry. Addition of GAPDH antibodies to cultured cerebellar neurons inhibited L1-dependent neurite outgrowth in the presence of ATP, while the application of exogenous GAPDH promoted L1-dependent neurite outgrowth. Pre-treatment of substrate-coated L1-Fc with ATP and GAPDH, which phosphorylates L1, subsequently led to an enhanced neurite outgrowth. Furthermore, aggregation of L1-Fc carrying beads was enhanced in the presence of both GAPDH and ATP. L1-dependent neurite outgrowth and aggregation of L1 were diminished in the presence of alkaline phosphatase or a protein kinase inhibitor. Our results show that GAPDH-dependent phosphorylation of L1 is a novel mechanism in regulating L1-mediated neurite outgrowth.

Original languageEnglish (US)
Pages (from-to)206-218
Number of pages13
JournalMolecular and Cellular Neuroscience
Issue number2
StatePublished - Jun 1 2009

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cellular and Molecular Neuroscience
  • Cell Biology


  • Adhesion molecule L1
  • Autophosphorylation
  • Extracellular
  • Fibronectin type III repeats
  • Immunoglobulin-like domains
  • Neurite outgrowth
  • Neuronal survival


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