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Dual regulation of neuronal morphogenesis by a delta-catenin-cortactin complex and Rho.

Martinez MC, Ochiishi T, Majewski M, Kosik KS - J. Cell Biol. (2003)

Bottom Line: Under conditions when tyrosine phosphorylation is reduced, delta-catenin binds to cortactin and cells extend unbranched primary processes.When RhoA is inhibited, delta-catenin enhances the effects of Rho inhibition on branching.We conclude that delta-catenin contributes to setting a balance between neurite elongation and branching in the elaboration of a complex dendritic tree.

View Article: PubMed Central - PubMed

Affiliation: Dept. of Neurology, Brigham and Women's Hospital and Harvard Medical School, Harvard Institute of Medicine, 77 Avenue Louis Pasteur, Boston, MA 02115, USA.

ABSTRACT
Delta-catenin is a neuronal protein that contains 10 Armadillo motifs and binds to the juxtamembrane segment of classical cadherins. We report that delta-catenin interacts with cortactin in a tyrosine phosphorylation-dependent manner. This interaction occurs within a region of the delta-catenin sequence that is also essential for the neurite elongation effects. Src family kinases can phosphorylate delta-catenin and bind to delta-catenin through its polyproline tract. Under conditions when tyrosine phosphorylation is reduced, delta-catenin binds to cortactin and cells extend unbranched primary processes. Conversely, increasing tyrosine phosphorylation disrupts the delta-catenin-cortactin complex. When RhoA is inhibited, delta-catenin enhances the effects of Rho inhibition on branching. We conclude that delta-catenin contributes to setting a balance between neurite elongation and branching in the elaboration of a complex dendritic tree.

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Inhibition of Src family kinases enhances δ-catenin– induced primary process elongation. (A) δ-PC12 cells were treated with 100 ng/ml NGF for 36 h and then left untreated (a) or treated with PP2 for 1 h (b). Cells were labeled with a mAb δ-catenin. Bar, 5 μm. (B) Quantification of neurite length and number of primary and secondary processes before and after PP2 treatment. No secondary processes were observed in the absence or presence of PP2.
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fig8: Inhibition of Src family kinases enhances δ-catenin– induced primary process elongation. (A) δ-PC12 cells were treated with 100 ng/ml NGF for 36 h and then left untreated (a) or treated with PP2 for 1 h (b). Cells were labeled with a mAb δ-catenin. Bar, 5 μm. (B) Quantification of neurite length and number of primary and secondary processes before and after PP2 treatment. No secondary processes were observed in the absence or presence of PP2.

Mentions: The inhibition of δ-catenin tyrosine phosphorylation in NGF-treated δ-PC12 cells exposed to PP2 (25 μM for 1 h) enhanced the morphological changes induced by δ-catenin (Fig. 8)Figure 8.


Dual regulation of neuronal morphogenesis by a delta-catenin-cortactin complex and Rho.

Martinez MC, Ochiishi T, Majewski M, Kosik KS - J. Cell Biol. (2003)

Inhibition of Src family kinases enhances δ-catenin– induced primary process elongation. (A) δ-PC12 cells were treated with 100 ng/ml NGF for 36 h and then left untreated (a) or treated with PP2 for 1 h (b). Cells were labeled with a mAb δ-catenin. Bar, 5 μm. (B) Quantification of neurite length and number of primary and secondary processes before and after PP2 treatment. No secondary processes were observed in the absence or presence of PP2.
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Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2172717&req=5

fig8: Inhibition of Src family kinases enhances δ-catenin– induced primary process elongation. (A) δ-PC12 cells were treated with 100 ng/ml NGF for 36 h and then left untreated (a) or treated with PP2 for 1 h (b). Cells were labeled with a mAb δ-catenin. Bar, 5 μm. (B) Quantification of neurite length and number of primary and secondary processes before and after PP2 treatment. No secondary processes were observed in the absence or presence of PP2.
Mentions: The inhibition of δ-catenin tyrosine phosphorylation in NGF-treated δ-PC12 cells exposed to PP2 (25 μM for 1 h) enhanced the morphological changes induced by δ-catenin (Fig. 8)Figure 8.

Bottom Line: Under conditions when tyrosine phosphorylation is reduced, delta-catenin binds to cortactin and cells extend unbranched primary processes.When RhoA is inhibited, delta-catenin enhances the effects of Rho inhibition on branching.We conclude that delta-catenin contributes to setting a balance between neurite elongation and branching in the elaboration of a complex dendritic tree.

View Article: PubMed Central - PubMed

Affiliation: Dept. of Neurology, Brigham and Women's Hospital and Harvard Medical School, Harvard Institute of Medicine, 77 Avenue Louis Pasteur, Boston, MA 02115, USA.

ABSTRACT
Delta-catenin is a neuronal protein that contains 10 Armadillo motifs and binds to the juxtamembrane segment of classical cadherins. We report that delta-catenin interacts with cortactin in a tyrosine phosphorylation-dependent manner. This interaction occurs within a region of the delta-catenin sequence that is also essential for the neurite elongation effects. Src family kinases can phosphorylate delta-catenin and bind to delta-catenin through its polyproline tract. Under conditions when tyrosine phosphorylation is reduced, delta-catenin binds to cortactin and cells extend unbranched primary processes. Conversely, increasing tyrosine phosphorylation disrupts the delta-catenin-cortactin complex. When RhoA is inhibited, delta-catenin enhances the effects of Rho inhibition on branching. We conclude that delta-catenin contributes to setting a balance between neurite elongation and branching in the elaboration of a complex dendritic tree.

Show MeSH
Related in: MedlinePlus