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. 2005 Dec;25(8):1225–1244. doi: 10.1007/s10571-005-8500-3

Subcellular Localization and Differentiation-Induced Redistribution of the Protein Tyrosine Phosphatase PTP-BL in Neuroblastoma Cells

Marco van Ham 1, Lottie Kemperman 1, Mietske Wijers 1, Jack Fransen 1, Wiljan Hendriks 1,2,✉
PMCID: PMC11529222  PMID: 16388334

Abstract

  1. In cells of epithelial origin the protein tyrosine phosphatase PTP-BL is predominantly localized at the apical membrane of polarized cells. This large submembranous multidomain PTP is also expressed in cells of neuronal origin. We studied the localization of PTP-BL in mouse neuroblastoma cells utilizing EGFP-tagged versions of the protein.

  2. In proliferating Neuro-2a cells, immunofluorescence and immuno-electron microscopy revealed a submembranous FERM domain-dependent localization at cell–cell boundaries for EGFP-PTP-BL. Additionally, significant amounts of EGFP-PTP-BL are located in the cytoplasm as well as in nuclei. Upon serum depletion-induced differentiation of Neuro-2a cells, a partial shift of EGFP-PTP-BL from a cortical localization to cytoskeleton-like F-actin-positive structures is observed. Parallel biochemical studies corroborate this finding and reveal a serum depletion-induced shift of EFGP-PTP-BL from a membrane(-associated) fraction to an NP40-soluble cytoskeletal fraction.

  3. Different pools of PTP-BL-containing protein complexes can be discerned in neuronal cells, reflecting distinct molecular microenvironments in which PTP-BL may exert its function.

Keywords: cytoskeleton, differentiation, FERM domain, PDZ domain, redistribution

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