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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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Cortactin binds to the COOH terminal region of δ-catenin. (A) COS1 cells were transfected with GFP–δ-catenin (FLδ), ΔC99 (top), ΔC205 (middle), and ΔC332 (bottom) constructs. Transfected cells were lysed and subjected to pull down with GST and GST–cortactin (GSTCort) constructs. (B) COS1 cells were transfected with either full-length δ-catenin (Flδ) or a full-length construct from which the polyproline tract was deleted (FLδΔP6), pulled down with GST or GST–cortactin, and blotted with mAb δ-catenin (top). COS1 cells were transfected with FLδ or ΔC99 and pulled down with GST or GST-cortactin, or GST–CTcortactin (GSTCtCort, aa 287–509 of cortactin), which retains the SH3 domain (bottom).
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fig5: Cortactin binds to the COOH terminal region of δ-catenin. (A) COS1 cells were transfected with GFP–δ-catenin (FLδ), ΔC99 (top), ΔC205 (middle), and ΔC332 (bottom) constructs. Transfected cells were lysed and subjected to pull down with GST and GST–cortactin (GSTCort) constructs. (B) COS1 cells were transfected with either full-length δ-catenin (Flδ) or a full-length construct from which the polyproline tract was deleted (FLδΔP6), pulled down with GST or GST–cortactin, and blotted with mAb δ-catenin (top). COS1 cells were transfected with FLδ or ΔC99 and pulled down with GST or GST-cortactin, or GST–CTcortactin (GSTCtCort, aa 287–509 of cortactin), which retains the SH3 domain (bottom).

Mentions: To determine the region in δ-catenin where cortactin binds, each of the δ-catenin deletion constructs (Fig. 3 A) was transfected into COS1 cells and pulled down with GST–cortactin (Fig. 5Figure 5.


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)

Cortactin binds to the COOH terminal region of δ-catenin. (A) COS1 cells were transfected with GFP–δ-catenin (FLδ), ΔC99 (top), ΔC205 (middle), and ΔC332 (bottom) constructs. Transfected cells were lysed and subjected to pull down with GST and GST–cortactin (GSTCort) constructs. (B) COS1 cells were transfected with either full-length δ-catenin (Flδ) or a full-length construct from which the polyproline tract was deleted (FLδΔP6), pulled down with GST or GST–cortactin, and blotted with mAb δ-catenin (top). COS1 cells were transfected with FLδ or ΔC99 and pulled down with GST or GST-cortactin, or GST–CTcortactin (GSTCtCort, aa 287–509 of cortactin), which retains the SH3 domain (bottom).
© Copyright Policy
Related In: Results  -  Collection

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

fig5: Cortactin binds to the COOH terminal region of δ-catenin. (A) COS1 cells were transfected with GFP–δ-catenin (FLδ), ΔC99 (top), ΔC205 (middle), and ΔC332 (bottom) constructs. Transfected cells were lysed and subjected to pull down with GST and GST–cortactin (GSTCort) constructs. (B) COS1 cells were transfected with either full-length δ-catenin (Flδ) or a full-length construct from which the polyproline tract was deleted (FLδΔP6), pulled down with GST or GST–cortactin, and blotted with mAb δ-catenin (top). COS1 cells were transfected with FLδ or ΔC99 and pulled down with GST or GST-cortactin, or GST–CTcortactin (GSTCtCort, aa 287–509 of cortactin), which retains the SH3 domain (bottom).
Mentions: To determine the region in δ-catenin where cortactin binds, each of the δ-catenin deletion constructs (Fig. 3 A) was transfected into COS1 cells and pulled down with GST–cortactin (Fig. 5Figure 5.

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