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LRRK2 and the stress response: interaction with MKKs and JNK-interacting proteins.

Increasing evidence supports a putative link between LRRK2 function and the MAP kinase cascades. We recently demonstrated that LRRK2 binds to MKK6, -3, and -7. Previous studies demonstrated that scaffold proteins are essential in the regulation of subcellular localization of stress kinase complexes. The c-jun NH2-terminal kinase (JNK)-interacting proteins (JIPs) are a group of scaffold proteins that play an important role in the regulation of MAP kinase signaling cascades. JIP1-3 are known to regulate the specificity and localization of the JNK pathway, while JIP4 is a specific scaffolding protein for the p38 pathway. We demonstrate that LRRK2 binds to JIP1-4, and is associated with increased levels of total JIP1, -3, -4, oligomeric JIP and ubiquitinated JIP. These results are consistent with a putative role of LRRK2 in regulating the stress kinase cascade.

Pubmed ID: 20173330

Authors

  • Hsu CH
  • Chan D
  • Wolozin B

Journal

Neuro-degenerative diseases

Publication Data

April 14, 2010

Associated Grants

  • Agency: NIEHS NIH HHS, Id: ES15567
  • Agency: NINDS NIH HHS, Id: NS060872
  • Agency: NIEHS NIH HHS, Id: R01 ES015567
  • Agency: NIEHS NIH HHS, Id: R01 ES015567-03
  • Agency: NIEHS NIH HHS, Id: R01 ES015567-04
  • Agency: NIEHS NIH HHS, Id: R01 ES015567-05
  • Agency: NINDS NIH HHS, Id: R01 NS060872
  • Agency: NINDS NIH HHS, Id: R01 NS060872-02S1
  • Agency: NINDS NIH HHS, Id: R01 NS060872-03
  • Agency: NINDS NIH HHS, Id: R01 NS060872-04

Mesh Terms

  • Analysis of Variance
  • Cell Line, Transformed
  • Humans
  • Immunoprecipitation
  • JNK Mitogen-Activated Protein Kinases
  • MAP Kinase Signaling System
  • Mutation
  • Oxidative Stress
  • Protein Binding
  • Protein-Serine-Threonine Kinases
  • Subcellular Fractions
  • Transfection