An inward rectifier K+ current modulates in neuroblastoma cells the tyrosine phosphorylation of the pp125FAK and associated proteins: Role in neuritogenesis

Laura Bianchi, Annarosa Arcangeli, Patrkia Bartolini, Gabriele Mugnai, Enzo Wanke, Massimo Olivotto

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


The relationships between the integrin-mediated activation of inward rectifyier K+ channels (K(IR)), the phosphorylation of pp125(FAK) and the rescue of neuritogenesis were studied in 41A3 mouse neuroblastoma cells. Neuritogenesis, elicited by adhesion to FN-enriched substrata, was reversibly impaired by pretreating these cells with the tyrosine kinase inhibitor Herbimycin A. This impairment mimicked that operated by Cs+ ions, which selectively inhibited the integrin-mediated activation of K(IR) channels. Various phosphotyrosine containing cellular proteins underwent a marked increase upon cell adhesion to FN-coated dishes. This increase was significantly reduced by Cs+ addition. Immunoprecipitation of pp125(FAK) revealed that the phosphorylation of this kinase and several associated proteins was significantly and reversibly inhibited by Cs+, indicating that integrin-mediated activation of K(IR) channels is a limiting step upstream to the phosphorylation of pp125(FAK) in the commitment to neuritogenesis.

Original languageEnglish (US)
Pages (from-to)823-829
Number of pages7
JournalBiochemical and biophysical research communications
Issue number3
StatePublished - May 25 1995
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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