Characterization of the zebrafish homolog of zipper interacting protein kinase
| Autor: | Tamara L Basepayne, Douglas C. Weiser, Brandon W. Carr, Vaishali Jayashankar, Lawrence Chen |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
MLC2
medicine.disease_cause lcsh:Chemistry 0302 clinical medicine DAPK3 lcsh:QH301-705.5 Peptide sequence Zebrafish Spectroscopy 0303 health sciences Mutation General Medicine Actomyosin Computer Science Applications Cell biology Actin Cytoskeleton 030220 oncology & carcinogenesis Phosphorylation animal structures Molecular Sequence Data Active Transport Cell Nucleus Biology Catalysis Article ZIPK Inorganic Chemistry 03 medical and health sciences Species Specificity Stress fiber medicine Animals Humans Amino Acid Sequence Physical and Theoretical Chemistry Mypt1 Protein kinase A Molecular Biology 030304 developmental biology Cell Nucleus Danio rerio Organic Chemistry HEK 293 cells Actin cytoskeleton biology.organism_classification Subcellular localization Death-Associated Protein Kinases HEK293 Cells lcsh:Biology (General) lcsh:QD1-999 HeLa Cells |
| Zdroj: | International Journal of Molecular Sciences Volume 15 Issue 7 Pages 11597-11613 International Journal of Molecular Sciences, Vol 15, Iss 7, Pp 11597-11613 (2014) |
| ISSN: | 1422-0067 |
| Popis: | Zipper-interacting protein kinase (ZIPK) is a conserved vertebrate-specific regulator of actomyosin contractility in smooth muscle and non-muscle cells. Murine ZIPK has undergone an unusual divergence in sequence and regulation compared to other ZIPK orthologs. In humans, subcellular localization is controlled by phosphorylation of threonines 299 and 300. In contrast, ZIPK subcellular localization in mouse and rat is controlled by interaction with PAR-4. We carried out a comparative biochemical characterization of the regulation of the zebrafish ortholog of ZIPK. Like the human orthologs zebrafish ZIPK undergoes nucleocytoplasmic-shuttling and is abundant in the cytoplasm, unlike the primarily nuclear rat ZIPK. Rat ZIPK, but not human or zebrafish ZIPK, interacts with zebrafish PAR-4. Mutation of the conserved residues required for activation of the mammalian orthologs abrogated activity of the zebrafish ZIPK. In contrast to the human ortholog, mutation of threonine 299 and 300 in the zebrafish ZIPK has no effect on the activity or subcellular localization. Thus, we found that zebrafish ZIPK functions in a manner most similar to the human ZIPK and quite distinct from murine orthologs, yet the regulation of subcellular localization is not conserved. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|