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Full-Text Articles in Chemistry
Tau-Tubulin Kinase 1 (Ttbk1), A Neuron-Specific Tau Kinase Candidate, Is Involved In Tau Phosphorylation And Aggregation, Shinji Sato, Ronald Cerny, James L. Buescher, Tsuneya Ikezu
Tau-Tubulin Kinase 1 (Ttbk1), A Neuron-Specific Tau Kinase Candidate, Is Involved In Tau Phosphorylation And Aggregation, Shinji Sato, Ronald Cerny, James L. Buescher, Tsuneya Ikezu
Ronald Cerny Publications
Neurofibrillary tangles, which are major pathological hallmarks of Alzheimer’s disease (AD), are composed of paired helical filaments (PHFs) containing hyperphosphorylated tau. Specific kinases regulate tau phosphorylation and are closely linked to the pathogenesis of AD. We have characterized a human tau-tubulin kinase 1 (TTBK1) gene located on chromosome 6p21.1. TTBK1 is a serine/threonine/tyrosine kinase that is conserved among species and belongs to the casein kinase 1 superfamily. It is specifically expressed in the brain, especially in the cytoplasm of cortical and hippocampal neurons. TTBK1 phosphorylates tau proteins in both a Mg2+- and a Mn2+-dependent manner. Phosphopeptide …
Protein–Protein Interactions Of Tandem Affinity Purification-Tagged Protein Kinases In Rice, Jai S. Rohila, Mei Chen, Shuo Chen, Johann Chen, Ronald Cerny, Chris Dardick, Patrick Canlas, Xia Xu, Michael Gribskov, Siddhartha Kanrar, Jian-Kang Zhu, P C. Ronald, Michael E. Fromm
Protein–Protein Interactions Of Tandem Affinity Purification-Tagged Protein Kinases In Rice, Jai S. Rohila, Mei Chen, Shuo Chen, Johann Chen, Ronald Cerny, Chris Dardick, Patrick Canlas, Xia Xu, Michael Gribskov, Siddhartha Kanrar, Jian-Kang Zhu, P C. Ronald, Michael E. Fromm
Ronald Cerny Publications
Forty-one rice cDNAs encoding protein kinases were fused to the tandem affinity purification (TAP) tag and expressed in transgenic rice plants. The TAP-tagged kinases and interacting proteins were purified from the T1 progeny of the transgenic rice plants and identified by mass spectrometry. Ninety-five percent of the TAP-tagged kinases were recovered. Fifty-six percent of the TAP-tagged kinases were found to interact with other rice proteins. A number of these interactions were consistent with known protein complexes found in other species, validating the TAP-tag method in rice plants. Phosphorylation sites were identified on four of the kinases that interacted with either …